Fibroblast growth factor receptor 2
Homo sapiens
State in the Current Structure
| Assembly | Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Associated Components | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|
| 1 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count | Chain A； UniProt 458–768 | Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768) Mutation：C491A, K659E | ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 SO4 SULFATE ION × 2 | X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, temperature 298K | Resolution 2.55 Å R-free 0.257 |
| 2 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count | Chain B； UniProt 458–768 | Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768) Mutation：C491A, K659E | ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 SO4 SULFATE ION × 1 | X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, temperature 298K | Resolution 2.55 Å R-free 0.257 |
| 3 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count | Chain C； UniProt 458–768 | Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768) Mutation：C491A, K659E | ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 SO4 SULFATE ION × 1 | X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, temperature 298K | Resolution 2.55 Å R-free 0.257 |
| 4 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count | Chain D； UniProt 458–768 | Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768) Mutation：C491A, K659E | ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 SO4 SULFATE ION × 1 | X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, temperature 298K | Resolution 2.55 Å R-free 0.257 |
| 5 | Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count | Chain A； UniProt 458–768 Chain C； UniProt 458–768 | Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768) Mutation：C491A, K659E | ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 2 SO4 SULFATE ION × 3 | X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, temperature 298K | Resolution 2.55 Å R-free 0.257 |
| 6 | Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count | Chain B； UniProt 458–768 Chain D； UniProt 458–768 | Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768) Mutation：C491A, K659E | ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 2 SO4 SULFATE ION × 2 | X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, temperature 298K | Resolution 2.55 Å R-free 0.257 |
Other States of the Same Protein in the Database
Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.
| Other PDB | Difference from Current Entry 4J97 | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 10OO FGFR2 mutant D650V with compound 4 (AZD3463) Deposited 2026-01-29 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
458–768（311 aa）
|
Mutation：D650V | A1C65 (4P)-N-[4-(4-aminopiperidin-1-yl)-2-methoxyphenyl]-5-chloro-4-(1H-indol-3-yl)pyrimidin-2-amine × 1 GOL GLYCEROL × 1 SO4 SULFATE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION；pH 8.5；293 K；30% PEG 4,000, 200 mM Lithium Sulfate, 100 mM TRIS pH 8.5
|
Resolution 1.85 Å R-free 0.256 |
| 10OO FGFR2 mutant D650V with compound 4 (AZD3463) Deposited 2026-01-29 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
458–768（311 aa）
|
Mutation：D650V | A1C65 (4P)-N-[4-(4-aminopiperidin-1-yl)-2-methoxyphenyl]-5-chloro-4-(1H-indol-3-yl)pyrimidin-2-amine × 1 SO4 SULFATE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION；pH 8.5；293 K；30% PEG 4,000, 200 mM Lithium Sulfate, 100 mM TRIS pH 8.5
|
Resolution 1.85 Å R-free 0.256 |
| 10OQ FGFR2 mutant D650V with compound 6 Deposited 2026-01-29 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
458–768（311 aa）
|
Mutation：D650V | A1C66 N-[(3M)-3-{5-chloro-2-[4-(morpholin-4-yl)anilino]pyrimidin-4-yl}-1-methyl-1H-indol-6-yl]propanamide × 1 GOL GLYCEROL × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION；pH 5.6；293 K；22% PEG 4,000, 200 mM Ammonium Sulfate, 100 mM Sodium Citrate pH 5.6
|
Resolution 1.98 Å R-free 0.251 |
| 10OQ FGFR2 mutant D650V with compound 6 Deposited 2026-01-29 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
458–768（311 aa）
|
Mutation：D650V | A1C66 N-[(3M)-3-{5-chloro-2-[4-(morpholin-4-yl)anilino]pyrimidin-4-yl}-1-methyl-1H-indol-6-yl]propanamide × 1 GOL GLYCEROL × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION；pH 5.6；293 K；22% PEG 4,000, 200 mM Ammonium Sulfate, 100 mM Sodium Citrate pH 5.6
|
Resolution 1.98 Å R-free 0.251 |
| 10OU FGFR2 mutant D650V with compound 12 Deposited 2026-01-29 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
458–768（311 aa）
|
Mutation：D650V | A1C67 N-[(3M)-3-{2-[(1-ethyl-1H-pyrazol-4-yl)amino]pyrimidin-4-yl}-1-methyl-1H-indol-6-yl]propanamide × 1 EDO 1,2-ETHANEDIOL × 11 GOL GLYCEROL × 4 SO4 SULFATE ION × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION；pH 5.6；293 K；22% PEG 4,000, 200 mM Ammonium Sulfate, 100 mM Sodium Citrate pH 5.6
|
Resolution 1.77 Å R-free 0.213 |
| 10OU FGFR2 mutant D650V with compound 12 Deposited 2026-01-29 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
458–768（311 aa）
|
Mutation：D650V | A1C67 N-[(3M)-3-{2-[(1-ethyl-1H-pyrazol-4-yl)amino]pyrimidin-4-yl}-1-methyl-1H-indol-6-yl]propanamide × 1 EDO 1,2-ETHANEDIOL × 11 GOL GLYCEROL × 8 SO4 SULFATE ION × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION；pH 5.6；293 K；22% PEG 4,000, 200 mM Ammonium Sulfate, 100 mM Sodium Citrate pH 5.6
|
Resolution 1.77 Å R-free 0.213 |
| 1DJS LIGAND-BINDING PORTION OF FIBROBLAST GROWTH FACTOR RECEPTOR 2 IN COMPLEX WITH FGF1 Deposited 1999-12-03 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain A
32–36（5 aa）
Fragment：IG-LIKE DOMAINS 2 AND 3
Chain A
152–362（211 aa）
Fragment：IG-LIKE DOMAINS 2 AND 3
|
Mutation：N147T,S148L,N149E,N150P,K151E,R152G Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：N147T,S148L,N149E,N150P,K151E,R152G Non-standard monomer：Yes (specific site not provided by mmCIF) | SO4 SULFATE ION × 18 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；1.6M AMMONIUM SULFATE, 10MM TRIS (PH7.5), pH 7.50
|
Resolution 2.40 Å R-free 0.315 |
| 1DJS LIGAND-BINDING PORTION OF FIBROBLAST GROWTH FACTOR RECEPTOR 2 IN COMPLEX WITH FGF1 Deposited 1999-12-03 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric |
Chain A
32–36（5 aa）
Fragment：IG-LIKE DOMAINS 2 AND 3
Chain A
152–362（211 aa）
Fragment：IG-LIKE DOMAINS 2 AND 3
|
Mutation：N147T,S148L,N149E,N150P,K151E,R152G Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：N147T,S148L,N149E,N150P,K151E,R152G Non-standard monomer：Yes (specific site not provided by mmCIF) | SO4 SULFATE ION × 36 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；1.6M AMMONIUM SULFATE, 10MM TRIS (PH7.5), pH 7.50
|
Resolution 2.40 Å R-free 0.315 |
| 1E0O CRYSTAL STRUCTURE OF A TERNARY FGF1-FGFR2-HEPARIN COMPLEX Deposited 2000-04-03 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: pentameric |
Chain B
148–366（219 aa）
Chain D
148–366（219 aa）
|
Not recorded | NI NICKEL (II) ION × 5 SO4 SULFATE ION × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 8.5；CRYSTALS WERE GROWN FROM: 1.0M LI2SO4, 0.1M TRISCL PH=8.5, 10MM NISO4, pH 8.50
|
Resolution 2.80 Å R-free 0.309 |
| 1EV2 CRYSTAL STRUCTURE OF FGF2 IN COMPLEX WITH THE EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 2 (FGFR2) Deposited 2000-04-19 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric |
Chain E
147–366（220 aa）
Fragment：EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 2 CONSISTING OF IMMUNOGLOBULIN LIKE DOMAINS II (D2) AND III (D3)
Chain F
147–366（220 aa）
Fragment：EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 2 CONSISTING OF IMMUNOGLOBULIN LIKE DOMAINS II (D2) AND III (D3)
Chain G
147–366（220 aa）
Fragment：EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 2 CONSISTING OF IMMUNOGLOBULIN LIKE DOMAINS II (D2) AND III (D3)
Chain H
147–366（220 aa）
Fragment：EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 2 CONSISTING OF IMMUNOGLOBULIN LIKE DOMAINS II (D2) AND III (D3)
|
Not recorded | SO4 SULFATE ION × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION；pH 7.5；298 K；PEG 4000, Isopropanol, HEPES-NaOH, pH 7.5, VAPOR DIFFUSION, temperature 298.0K
|
Resolution 2.20 Å R-free 0.273 |
| 1GJO The FGFr2 tyrosine kinase domain Deposited 2001-07-31 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
456–768（313 aa）
Fragment：TYROSINE KINASE DOMAIN RESIDUES 465-768
|
Not recorded | SO4 SULFATE ION × 8 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 5.9；32% AMMONIUM SULFATE, TRIS/MALEIC ACID BUFFER, PH 5.9
|
Resolution 2.40 Å R-free 0.256 |
| 1II4 CRYSTAL STRUCTURE OF SER252TRP APERT MUTANT FGF RECEPTOR 2 (FGFR2) IN COMPLEX WITH FGF2 Deposited 2001-04-20 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain E
147–366（220 aa）
Fragment：EXTRACELLULAR LIGAND BINDING DOMAIN CONSISTING OF IG-LIKE DOMAINS II (D2) AND III (D3), RESIDUES 147-366
|
Mutation：S252W | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；PEG 4000, Isopropanol, HEPES-NaOH, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
|
Resolution 2.70 Å R-free 0.267 |
| 1II4 CRYSTAL STRUCTURE OF SER252TRP APERT MUTANT FGF RECEPTOR 2 (FGFR2) IN COMPLEX WITH FGF2 Deposited 2001-04-20 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain F
147–366（220 aa）
Fragment：EXTRACELLULAR LIGAND BINDING DOMAIN CONSISTING OF IG-LIKE DOMAINS II (D2) AND III (D3), RESIDUES 147-366
|
Mutation：S252W | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；PEG 4000, Isopropanol, HEPES-NaOH, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
|
Resolution 2.70 Å R-free 0.267 |
| 1II4 CRYSTAL STRUCTURE OF SER252TRP APERT MUTANT FGF RECEPTOR 2 (FGFR2) IN COMPLEX WITH FGF2 Deposited 2001-04-20 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain G
147–366（220 aa）
Fragment：EXTRACELLULAR LIGAND BINDING DOMAIN CONSISTING OF IG-LIKE DOMAINS II (D2) AND III (D3), RESIDUES 147-366
|
Mutation：S252W | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；PEG 4000, Isopropanol, HEPES-NaOH, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
|
Resolution 2.70 Å R-free 0.267 |
| 1II4 CRYSTAL STRUCTURE OF SER252TRP APERT MUTANT FGF RECEPTOR 2 (FGFR2) IN COMPLEX WITH FGF2 Deposited 2001-04-20 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain H
147–366（220 aa）
Fragment：EXTRACELLULAR LIGAND BINDING DOMAIN CONSISTING OF IG-LIKE DOMAINS II (D2) AND III (D3), RESIDUES 147-366
|
Mutation：S252W | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；PEG 4000, Isopropanol, HEPES-NaOH, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
|
Resolution 2.70 Å R-free 0.267 |
| 1IIL CRYSTAL STRUCTURE OF PRO253ARG APERT MUTANT FGF RECEPTOR 2 (FGFR2) IN COMPLEX WITH FGF2 Deposited 2001-04-23 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain E
147–366（220 aa）
Fragment：EXTRACELLULAR LIGAND BINDING DOMAIN CONSISTING OF IG-LIKE DOMAINS II (D2) AND III (D3), RESIDUES 147-366
|
Mutation：P253R | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；PEG 4000, Isopropanol, HEPES-NaOH, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
|
Resolution 2.30 Å R-free 0.259 |
| 1IIL CRYSTAL STRUCTURE OF PRO253ARG APERT MUTANT FGF RECEPTOR 2 (FGFR2) IN COMPLEX WITH FGF2 Deposited 2001-04-23 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain F
147–366（220 aa）
Fragment：EXTRACELLULAR LIGAND BINDING DOMAIN CONSISTING OF IG-LIKE DOMAINS II (D2) AND III (D3), RESIDUES 147-366
|
Mutation：P253R | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；PEG 4000, Isopropanol, HEPES-NaOH, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
|
Resolution 2.30 Å R-free 0.259 |
| 1IIL CRYSTAL STRUCTURE OF PRO253ARG APERT MUTANT FGF RECEPTOR 2 (FGFR2) IN COMPLEX WITH FGF2 Deposited 2001-04-23 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain G
147–366（220 aa）
Fragment：EXTRACELLULAR LIGAND BINDING DOMAIN CONSISTING OF IG-LIKE DOMAINS II (D2) AND III (D3), RESIDUES 147-366
|
Mutation：P253R | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；PEG 4000, Isopropanol, HEPES-NaOH, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
|
Resolution 2.30 Å R-free 0.259 |
| 1IIL CRYSTAL STRUCTURE OF PRO253ARG APERT MUTANT FGF RECEPTOR 2 (FGFR2) IN COMPLEX WITH FGF2 Deposited 2001-04-23 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain H
147–366（220 aa）
Fragment：EXTRACELLULAR LIGAND BINDING DOMAIN CONSISTING OF IG-LIKE DOMAINS II (D2) AND III (D3), RESIDUES 147-366
|
Mutation：P253R | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；PEG 4000, Isopropanol, HEPES-NaOH, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
|
Resolution 2.30 Å R-free 0.259 |
| 1NUN Crystal Structure Analysis of the FGF10-FGFR2b Complex Deposited 2003-01-31 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain B
140–369（230 aa）
|
Non-standard monomer：Yes (specific site not provided by mmCIF) | SO4 SULFATE ION × 2 15P POLYETHYLENE GLYCOL (N=34) × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；PEG 400, ammonium sulfate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.90 Å R-free 0.288 |
| 1OEC FGFr2 kinase domain Deposited 2003-03-24 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
456–768（313 aa）
Fragment：TYROSINE KINASE DOMAIN, RESIDUES 456-768
|
Not recorded | SO4 SULFATE ION × 8 AA2 4-ARYL-2-PHENYLAMINO PYRIMIDINE × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 5.9；pH 5.90
|
Resolution 2.40 Å R-free 0.285 |
| 2PSQ Crystal Structure of Unphosphorylated Unactivated Wild Type FGF Receptor 2 (FGFR2) Kinase Domain Deposited 2007-05-07 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
413–768（356 aa）
Fragment：Kinase Domain
Chain B
413–768（356 aa）
Fragment：Kinase Domain
|
Not recorded | SO4 SULFATE ION × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 20% PEG 4000, 200mM (NH4)2SO4, 3% C2H4O, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.40 Å R-free 0.258 |
| 2PVF Crystal Structure of Tyrosine Phosphorylated Activated FGF Receptor 2 (FGFR2) Kinase Domain in Complex with ATP Analog and Substrate Peptide Deposited 2007-05-09 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
458–778（321 aa）
Fragment：human FGF Receptor 2 Kinase Domain
Chain B
764–778（15 aa）
Fragment：Peptide Stubstrate
|
Mutation：C491A Non-standard monomer：Yes (specific site not provided by mmCIF) | MG MAGNESIUM ION × 2 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 27% PEG 4000, 200mM (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 1.80 Å R-free 0.265 |
| 2PVY Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic K659N Mutation Responsible for an Unclassified Craniosynostosis Syndrome. Deposited 2007-05-10 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
458–768（311 aa）
Fragment：Kinase Domain
Chain B
458–768（311 aa）
Fragment：Kinase Domain
Chain C
458–768（311 aa）
Fragment：Kinase Domain
Chain D
458–768（311 aa）
Fragment：Kinase Domain
|
Mutation：C491A, K659N Mutation：C491A, K659N Mutation：C491A, K659N Mutation：C491A, K659N | SO4 SULFATE ION × 4 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.20 Å R-free 0.276 |
| 2PWL Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic N549H Mutation Responsible for Crouzon Syndrome. Deposited 2007-05-11 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
458–768（311 aa）
Fragment：Kinase Domain
Chain B
458–768（311 aa）
Fragment：Kinase Domain
|
Mutation：C491A, N549H Mutation：C491A, N549H | SO4 SULFATE ION × 4 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, 8% C3H5(OH)3, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.40 Å R-free 0.238 |
| 2PY3 Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic E565G Mutation Responsible for Pfeiffer Syndrome Deposited 2007-05-15 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
458–768（311 aa）
Fragment：Kinase Domain
Chain B
458–768（311 aa）
Fragment：Kinase Domain
|
Mutation：C491A, E565G Mutation：C491A, E565G | SO4 SULFATE ION × 4 MG MAGNESIUM ION × 4 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, 2% C3H5(OH)3, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.30 Å R-free 0.252 |
| 2PZ5 Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic N549T Mutation Responsible for Pfeiffer Syndrome Deposited 2007-05-17 | Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
458–768（311 aa）
Fragment：Kinase Domain
Chain B
458–768（311 aa）
Fragment：Kinase Domain
|
Mutation：C491A, N549T Mutation：C491A, N549T | SO4 SULFATE ION × 4 MG MAGNESIUM ION × 4 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.40 Å R-free 0.254 |
| 2PZP Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic K526E Mutation Responsible for Crouzon Syndrome Deposited 2007-05-18 | Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
458–768（311 aa）
Fragment：Kinase Domain
Chain B
458–768（311 aa）
Fragment：Kinase Domain
|
Mutation：C491A, K526E Mutation：C491A, K526E | SO4 SULFATE ION × 4 MG MAGNESIUM ION × 4 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.40 Å R-free 0.251 |
| 2PZR Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic K641R Mutation Responsible for Pfeiffer Syndrome Deposited 2007-05-18 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
458–768（311 aa）
Fragment：Kinase Domain
Chain B
458–768（311 aa）
Fragment：Kinase Domain
|
Mutation：C491A, K641R Mutation：C491A, K641R | SO4 SULFATE ION × 4 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 28% PEG 4000, 300mM (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 3.00 Å R-free 0.268 |
| 2Q0B Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic E565A Mutation Responsible for Pfeiffer Syndrome Deposited 2007-05-21 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
458–768（311 aa）
Fragment：Kinase Domain
Chain B
458–768（311 aa）
Fragment：Kinase Domain
|
Mutation：C491A, E565A Mutation：C491A, E565A | SO4 SULFATE ION × 4 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 19% PEG 4000, 300mM (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.90 Å R-free 0.252 |
| 3B2T Structure of phosphotransferase Deposited 2007-10-19 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
458–768（311 aa）
Fragment：UNP residues 458-768
Chain B
458–768（311 aa）
Fragment：UNP residues 458-768
|
Mutation：A628T, E767Q Mutation：A628T, E767Q | PO4 PHOSPHATE ION × 8 M33 5'-O-[(S)-hydroxy{[(S)-hydroxy(methyl)phosphoryl]oxy}phosphoryl]adenosine × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；277 K；0.6M sodium dihydrogen phosphate, 0.6M potassium dihydrogen phosphate, 0.1M HEPES, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.80 Å R-free 0.233 |
| 3B2T Structure of phosphotransferase Deposited 2007-10-19 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
458–768（311 aa）
Fragment：UNP residues 458-768
Chain B
458–768（311 aa）
Fragment：UNP residues 458-768
|
Mutation：A628T, E767Q Mutation：A628T, E767Q | PO4 PHOSPHATE ION × 4 M33 5'-O-[(S)-hydroxy{[(S)-hydroxy(methyl)phosphoryl]oxy}phosphoryl]adenosine × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；277 K；0.6M sodium dihydrogen phosphate, 0.6M potassium dihydrogen phosphate, 0.1M HEPES, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.80 Å R-free 0.233 |
| 3CAF Crystal Structure of hFGFR2 D2 Domain Deposited 2008-02-19 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
150–249（100 aa）
Fragment：Ig-like C2-type 2
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；20%(w/v) PEG3350, 0.1M (NH3)2SO4, 100mM HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 1.96 Å R-free 0.275 |
| 3CAF Crystal Structure of hFGFR2 D2 Domain Deposited 2008-02-19 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
150–249（100 aa）
Fragment：Ig-like C2-type 2
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；20%(w/v) PEG3350, 0.1M (NH3)2SO4, 100mM HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 1.96 Å R-free 0.275 |
| 3CLY Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domains Trapped in Trans-Phosphorylation Reaction Deposited 2008-03-20 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
458–778（321 aa）
Fragment：Protein Kinase Domain
|
Mutation：C491A Non-standard monomer：Yes (specific site not provided by mmCIF) | MG MAGNESIUM ION × 4 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100 mM HEPES pH7.5, 26% PEG 4000, 200 mM (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.00 Å R-free 0.247 |
| 3CLY Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domains Trapped in Trans-Phosphorylation Reaction Deposited 2008-03-20 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
458–778（321 aa）
Fragment：Protein Kinase Domain
|
Mutation：C491A Non-standard monomer：Yes (specific site not provided by mmCIF) | MG MAGNESIUM ION × 2 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100 mM HEPES pH7.5, 26% PEG 4000, 200 mM (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.00 Å R-free 0.247 |
| 3CU1 Crystal Structure of 2:2:2 FGFR2D2:FGF1:SOS complex Deposited 2008-04-15 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain A
150–249（100 aa）
Fragment：Ig-like C2-type 2 domain, UNP residues 150-249
Chain C
150–249（100 aa）
Fragment：Ig-like C2-type 2 domain, UNP residues 150-249
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；12% PEG3350, 4% Tacsimate, pH 7.0, vapor diffusion, hanging drop, temperature 298.0K
|
Resolution 2.60 Å R-free 0.277 |
| 3DAR Crystal structure of D2 domain from human FGFR2 Deposited 2008-05-30 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
146–249（104 aa）
Fragment：D2 domain, Ig-like C2-type 2, UNP residues 146-249
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；291 K；0.2 M sodium acetate, 0.1 M Tris-HCl, 30% PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 291.0K, pH 8.5
|
Resolution 2.20 Å R-free 0.255 |
| 3DAR Crystal structure of D2 domain from human FGFR2 Deposited 2008-05-30 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
146–249（104 aa）
Fragment：D2 domain, Ig-like C2-type 2, UNP residues 146-249
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；291 K；0.2 M sodium acetate, 0.1 M Tris-HCl, 30% PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 291.0K, pH 8.5
|
Resolution 2.20 Å R-free 0.255 |
| 3EUU Crystal structure of the FGFR2 D2 domain Deposited 2008-10-10 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
150–249（100 aa）
Fragment：UNP residues 150-249
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；1.8M ammonium citrate dibasic, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.34 Å R-free 0.228 |
| 3EUU Crystal structure of the FGFR2 D2 domain Deposited 2008-10-10 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
150–249（100 aa）
Fragment：UNP residues 150-249
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；1.8M ammonium citrate dibasic, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.34 Å R-free 0.228 |
| 3EUU Crystal structure of the FGFR2 D2 domain Deposited 2008-10-10 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
150–249（100 aa）
Fragment：UNP residues 150-249
Chain B
150–249（100 aa）
Fragment：UNP residues 150-249
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；1.8M ammonium citrate dibasic, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.34 Å R-free 0.228 |
| 3OJ2 Crystal structure of FGF1 complexed with the ectodomain of FGFR2b harboring the A172F Pfeiffer syndrome mutation Deposited 2010-08-20 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain C
140–313（174 aa）
|
Mutation：A172F | SO4 SULFATE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；0.1M Hepes, 20% PEG4000, 0.2M ammonium sulfate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.20 Å R-free 0.294 |
| 3OJ2 Crystal structure of FGF1 complexed with the ectodomain of FGFR2b harboring the A172F Pfeiffer syndrome mutation Deposited 2010-08-20 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain D
140–313（174 aa）
|
Mutation：A172F | SO4 SULFATE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；0.1M Hepes, 20% PEG4000, 0.2M ammonium sulfate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.20 Å R-free 0.294 |
| 3OJM Crystal Structure of FGF1 complexed with the ectodomain of FGFR2b harboring P253R Apert mutation Deposited 2010-08-23 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain B
140–313（174 aa）
Fragment：FGFR2b
|
Mutation：P253R | SO4 SULFATE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；0.1M Hepes, 22% monomethyl ether PEG5000, 0.2M ammonium sulfate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.10 Å R-free 0.263 |
| 3RI1 Crystal structure of the catalytic domain of FGFR2 kinase in complex with ARQ 069 Deposited 2011-04-12 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
458–768（311 aa）
Fragment：UNP residues 458-768
|
Not recorded | 3RH (6S)-6-phenyl-5,6-dihydrobenzo[h]quinazolin-2-amine × 1 SO4 SULFATE ION × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；15% polyethylene glycol 4000 and 0.3M lithium sulfate and 100 mM HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.10 Å R-free 0.247 |
| 3RI1 Crystal structure of the catalytic domain of FGFR2 kinase in complex with ARQ 069 Deposited 2011-04-12 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
458–768（311 aa）
Fragment：UNP residues 458-768
|
Not recorded | 3RH (6S)-6-phenyl-5,6-dihydrobenzo[h]quinazolin-2-amine × 1 SO4 SULFATE ION × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；15% polyethylene glycol 4000 and 0.3M lithium sulfate and 100 mM HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.10 Å R-free 0.247 |
| 4J23 Low resolution crystal structure of the FGFR2D2D3/FGF1/SR128545 complex Deposited 2013-02-04 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain A
147–366（220 aa）
Fragment：unp residues 147-366
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 3.88 Å R-free 0.384 |
| 4J95 Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic K659N Mutation Responsible for an Unclassified Craniosynostosis Syndrome in Space Group C2. Deposited 2013-02-15 | Different mutation/modification Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
458–768（311 aa）
Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768)
|
Mutation：C491A, K659N | ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 SO4 SULFATE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, 3% v/v CH3CH2OH, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.38 Å R-free 0.255 |
| 4J95 Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic K659N Mutation Responsible for an Unclassified Craniosynostosis Syndrome in Space Group C2. Deposited 2013-02-15 | Different mutation/modification Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
458–768（311 aa）
Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768)
|
Mutation：C491A, K659N | ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, 3% v/v CH3CH2OH, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.38 Å R-free 0.255 |
| 4J95 Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic K659N Mutation Responsible for an Unclassified Craniosynostosis Syndrome in Space Group C2. Deposited 2013-02-15 | Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
458–768（311 aa）
Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768)
|
Mutation：C491A, K659N | ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 SO4 SULFATE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, 3% v/v CH3CH2OH, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.38 Å R-free 0.255 |
| 4J95 Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic K659N Mutation Responsible for an Unclassified Craniosynostosis Syndrome in Space Group C2. Deposited 2013-02-15 | Different mutation/modification Different experimental conditions Different structure-quality metrics | Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain D
458–768（311 aa）
Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768)
|
Mutation：C491A, K659N | ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, 3% v/v CH3CH2OH, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.38 Å R-free 0.255 |
| 4J95 Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic K659N Mutation Responsible for an Unclassified Craniosynostosis Syndrome in Space Group C2. Deposited 2013-02-15 | Different mutation/modification Different experimental conditions Different structure-quality metrics | Assembly 5 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
458–768（311 aa）
Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768)
Chain B
458–768（311 aa）
Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768)
|
Mutation：C491A, K659N Mutation：C491A, K659N | ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 2 SO4 SULFATE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, 3% v/v CH3CH2OH, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.38 Å R-free 0.255 |
| 4J95 Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic K659N Mutation Responsible for an Unclassified Craniosynostosis Syndrome in Space Group C2. Deposited 2013-02-15 | Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 6 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain C
458–768（311 aa）
Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768)
Chain D
458–768（311 aa）
Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768)
|
Mutation：C491A, K659N Mutation：C491A, K659N | ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 2 SO4 SULFATE ION × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, 3% v/v CH3CH2OH, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.38 Å R-free 0.255 |
| 4J96 Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic Gain-of-Function K659M Mutation Identified in Cervical Cancer. Deposited 2013-02-15 | Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
458–768（311 aa）
Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768)
|
Mutation：C491A, K659M | SO4 SULFATE ION × 1 FLC CITRATE ANION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, 100mM HOC(COONa)(CH2COONa)2, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.30 Å R-free 0.219 |
| 4J96 Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic Gain-of-Function K659M Mutation Identified in Cervical Cancer. Deposited 2013-02-15 | Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
458–768（311 aa）
Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768)
|
Mutation：C491A, K659M | SO4 SULFATE ION × 2 FLC CITRATE ANION × 1 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, 100mM HOC(COONa)(CH2COONa)2, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.30 Å R-free 0.219 |
| 4J96 Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic Gain-of-Function K659M Mutation Identified in Cervical Cancer. Deposited 2013-02-15 | Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
458–768（311 aa）
Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768)
Chain B
458–768（311 aa）
Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768)
|
Mutation：C491A, K659M Mutation：C491A, K659M | SO4 SULFATE ION × 3 FLC CITRATE ANION × 2 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, 100mM HOC(COONa)(CH2COONa)2, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.30 Å R-free 0.219 |
| 4J98 Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Gain-of-Function K659Q Mutation. Deposited 2013-02-15 | Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
458–768（311 aa）
Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768)
|
Mutation：C491A, K659Q | SO4 SULFATE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, 100mM HOC(COONa)(CH2COONa)2, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.31 Å R-free 0.234 |
| 4J98 Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Gain-of-Function K659Q Mutation. Deposited 2013-02-15 | Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
458–768（311 aa）
Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768)
|
Mutation：C491A, K659Q | SO4 SULFATE ION × 3 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, 100mM HOC(COONa)(CH2COONa)2, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.31 Å R-free 0.234 |
| 4J98 Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Gain-of-Function K659Q Mutation. Deposited 2013-02-15 | Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
458–768（311 aa）
Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768)
Chain B
458–768（311 aa）
Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768)
|
Mutation：C491A, K659Q Mutation：C491A, K659Q | SO4 SULFATE ION × 5 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, 100mM HOC(COONa)(CH2COONa)2, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.31 Å R-free 0.234 |
| 4J99 Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Gain-of-Function K659T Mutation. Deposited 2013-02-15 | Different mutation/modification Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
458–768（311 aa）
Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768)
|
Mutation：C491A, K659T | SO4 SULFATE ION × 2 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, 100mM KCl, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 1.85 Å R-free 0.240 |
| 4J99 Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Gain-of-Function K659T Mutation. Deposited 2013-02-15 | Different mutation/modification Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
458–768（311 aa）
Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768)
|
Mutation：C491A, K659T | SO4 SULFATE ION × 2 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, 100mM KCl, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 1.85 Å R-free 0.240 |
| 4J99 Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Gain-of-Function K659T Mutation. Deposited 2013-02-15 | Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
458–768（311 aa）
Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768)
|
Mutation：C491A, K659T | SO4 SULFATE ION × 2 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, 100mM KCl, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 1.85 Å R-free 0.240 |
| 4J99 Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Gain-of-Function K659T Mutation. Deposited 2013-02-15 | Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain D
458–768（311 aa）
Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768)
|
Mutation：C491A, K659T | SO4 SULFATE ION × 1 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 MG MAGNESIUM ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, 100mM KCl, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 1.85 Å R-free 0.240 |
| 4J99 Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Gain-of-Function K659T Mutation. Deposited 2013-02-15 | Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 5 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
458–768（311 aa）
Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768)
Chain B
458–768（311 aa）
Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768)
|
Mutation：C491A, K659T Mutation：C491A, K659T | SO4 SULFATE ION × 4 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, 100mM KCl, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 1.85 Å R-free 0.240 |
| 4J99 Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Gain-of-Function K659T Mutation. Deposited 2013-02-15 | Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 6 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain C
458–768（311 aa）
Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768)
Chain D
458–768（311 aa）
Fragment：Human FGF Receptor 2 Kinase Domain (UNP Residues 458-768)
|
Mutation：C491A, K659T Mutation：C491A, K659T | SO4 SULFATE ION × 3 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 2 MG MAGNESIUM ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM HEPES pH7.5, 25% PEG 4000, 200mM (NH4)2SO4, 100mM KCl, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 1.85 Å R-free 0.240 |
| 4WV1 Crystal structure of the FGFR2 D2 domain in complex with Fab 2B.1.3 Deposited 2014-11-04 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain F
153–251（99 aa）
Fragment：UNP residues 153-251
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；292 K；PEG 3350, potassium nitrate
|
Resolution 2.36 Å R-free 0.244 |
| 4WV1 Crystal structure of the FGFR2 D2 domain in complex with Fab 2B.1.3 Deposited 2014-11-04 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain C
153–251（99 aa）
Fragment：UNP residues 153-251
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；292 K；PEG 3350, potassium nitrate
|
Resolution 2.36 Å R-free 0.244 |
| 5EG3 Crystal Structure of the Activated FGF Receptor 2 (FGFR2) Kinase Domain in complex with the cSH2 domain of Phospholipase C gamma (PLCgamma) Deposited 2015-10-26 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain A
458–778（321 aa）
Fragment：UNP residues 458-778
|
Mutation：Y466F, C491A, E565A, Y586L, Y588P, Y656F, Y657F, K659E Non-standard monomer：Yes (specific site not provided by mmCIF) | ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 MG MAGNESIUM ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；25 mM HEPES (pH 7.5), PEG20000 (12% 18%) and 2% (w/v) Benzamidine hydrochloride
|
Resolution 2.61 Å R-free 0.237 |
| 5UGL Crystal Structure of FGF Receptor 2 Tyrosine Kinase Domain Harboring the D650V Activating Mutation Deposited 2017-01-09 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
341–651（311 aa）
Fragment：UNP residues 341-651
|
Mutation：D650V | SO4 SULFATE ION × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；293 K；25 mM HEPES pH7.5, 15%-25% w/v PEG4000, 0.2-0.3 M NH4SO3
|
Resolution 1.86 Å R-free 0.258 |
| 5UGL Crystal Structure of FGF Receptor 2 Tyrosine Kinase Domain Harboring the D650V Activating Mutation Deposited 2017-01-09 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
341–651（311 aa）
Fragment：UNP residues 341-651
|
Mutation：D650V | SO4 SULFATE ION × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；293 K；25 mM HEPES pH7.5, 15%-25% w/v PEG4000, 0.2-0.3 M NH4SO3
|
Resolution 1.86 Å R-free 0.258 |
| 5UGX Crystal Structure of the Tyrosine Kinase Domain of FGF Receptor 2 Harboring a E565A/D650V double Gain-of-Function Mutation Deposited 2017-01-10 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
341–651（311 aa）
Fragment：UNP residues 341-651
|
Mutation：E565A, D650V | SO4 SULFATE ION × 2 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；293 K；25 mM HEPES (pH 7.5), 15%-25% w/v PEG 4000, 0.2-0.3 M Ammonium sulfate
|
Resolution 2.35 Å R-free 0.275 |
| 5UGX Crystal Structure of the Tyrosine Kinase Domain of FGF Receptor 2 Harboring a E565A/D650V double Gain-of-Function Mutation Deposited 2017-01-10 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
341–651（311 aa）
Fragment：UNP residues 341-651
|
Mutation：E565A, D650V | SO4 SULFATE ION × 2 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；293 K；25 mM HEPES (pH 7.5), 15%-25% w/v PEG 4000, 0.2-0.3 M Ammonium sulfate
|
Resolution 2.35 Å R-free 0.275 |
| 5UHN Crystal Structure of the Tyrosine Kinase Domain of FGF Receptor 2 harboring a N549H/E565A Double Gain-of-Function Mutation Deposited 2017-01-11 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
342–652（311 aa）
Fragment：UNP residues 342-652
|
Mutation：N549H, E565A | SO4 SULFATE ION × 1 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；293 K；25 mM HEPES (pH 7.5), 15-25% w/v PEG 4000, 0.2-0.3 M Ammonium Sulfate
|
Resolution 2.91 Å R-free 0.311 |
| 5UHN Crystal Structure of the Tyrosine Kinase Domain of FGF Receptor 2 harboring a N549H/E565A Double Gain-of-Function Mutation Deposited 2017-01-11 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
342–652（311 aa）
Fragment：UNP residues 342-652
|
Mutation：N549H, E565A | SO4 SULFATE ION × 1 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；293 K；25 mM HEPES (pH 7.5), 15-25% w/v PEG 4000, 0.2-0.3 M Ammonium Sulfate
|
Resolution 2.91 Å R-free 0.311 |
| 5UI0 Crystal Structure of the Tyrosine Kinase Domain of FGF Receptor 2 harboring an E565A/K659M Double Gain-of-Function Mutation Deposited 2017-01-12 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
341–651（311 aa）
Fragment：UNP residues 341-651
|
Mutation：E565A, K659M | FLC CITRATE ANION × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；293 K；25 mM HEPES pH 7.5, 15%-25% w/v PEG 4000, 0.2-0.3 M Ammonium Sulfate
|
Resolution 2.05 Å R-free 0.207 |
| 5UI0 Crystal Structure of the Tyrosine Kinase Domain of FGF Receptor 2 harboring an E565A/K659M Double Gain-of-Function Mutation Deposited 2017-01-12 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
341–651（311 aa）
Fragment：UNP residues 341-651
|
Mutation：E565A, K659M | FLC CITRATE ANION × 1 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；293 K；25 mM HEPES pH 7.5, 15%-25% w/v PEG 4000, 0.2-0.3 M Ammonium Sulfate
|
Resolution 2.05 Å R-free 0.207 |
| 6AGX The cocrystal structure of FGFR2 bound with compound 14 harboring 5H-pyrrolo[2,3-b]pyrazine scaffold Deposited 2018-08-15 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
467–764（298 aa）
Fragment：UNP residues 467-764
Chain B
467–764（298 aa）
Fragment：UNP residues 467-764
|
Mutation：A628T Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：A628T Non-standard monomer：Yes (specific site not provided by mmCIF) | 9WX ethyl [4-({3-[2-(3,5-dimethoxyphenyl)ethyl]-5H-pyrrolo[2,3-b]pyrazin-5-yl}sulfonyl)-1H-imidazol-1-yl]acetate × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
EVAPORATION；pH 6.5；298 K；0.2M Ammonium sulfate, 0.1M MES pH 6.5, 30%(w/v) PEG 5000 MME
|
Resolution 2.95 Å R-free 0.298 |
| 6AGX The cocrystal structure of FGFR2 bound with compound 14 harboring 5H-pyrrolo[2,3-b]pyrazine scaffold Deposited 2018-08-15 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain C
467–764（298 aa）
Fragment：UNP residues 467-764
Chain D
467–764（298 aa）
Fragment：UNP residues 467-764
|
Mutation：A628T Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：A628T Non-standard monomer：Yes (specific site not provided by mmCIF) | 9WX ethyl [4-({3-[2-(3,5-dimethoxyphenyl)ethyl]-5H-pyrrolo[2,3-b]pyrazin-5-yl}sulfonyl)-1H-imidazol-1-yl]acetate × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
EVAPORATION；pH 6.5；298 K；0.2M Ammonium sulfate, 0.1M MES pH 6.5, 30%(w/v) PEG 5000 MME
|
Resolution 2.95 Å R-free 0.298 |
| 6LVK Crystal structure of FGFR2 in complex with 1,3,5-triazine derivative Deposited 2020-02-04 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
459–768（310 aa）
|
Non-standard monomer：Yes (specific site not provided by mmCIF) | EVC N-ethyl-2-[[4-[[4-(4-methylpiperazin-1-yl)-3-(2-morpholin-4-ylethoxy)phenyl]amino]-1,3,5-triazin-2-yl]amino]benzenesulfonamide × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 8.5；296 K；Tris, Ammonium sulfate, PEG 8000
|
Resolution 2.29 Å R-free 0.247 |
| 6LVK Crystal structure of FGFR2 in complex with 1,3,5-triazine derivative Deposited 2020-02-04 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
459–768（310 aa）
|
Non-standard monomer：Yes (specific site not provided by mmCIF) | EVC N-ethyl-2-[[4-[[4-(4-methylpiperazin-1-yl)-3-(2-morpholin-4-ylethoxy)phenyl]amino]-1,3,5-triazin-2-yl]amino]benzenesulfonamide × 1 SO4 SULFATE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 8.5；296 K；Tris, Ammonium sulfate, PEG 8000
|
Resolution 2.29 Å R-free 0.247 |
| 6LVL Crystal structure of FGFR2 in complex with 1,3,5-triazine derivative Deposited 2020-02-04 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
459–768（310 aa）
|
Not recorded | SO4 SULFATE ION × 1 EVL N-ethyl-2-[[4-[[3-methoxy-4-[4-(4-methylpiperazin-1-yl)piperidin-1-yl]phenyl]amino]-1,3,5-triazin-2-yl]amino]benzenesulfonamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 8.5；296 K；Tris, Ammonium sulfate, PEG 8000
|
Resolution 2.98 Å R-free 0.251 |
| 6LVL Crystal structure of FGFR2 in complex with 1,3,5-triazine derivative Deposited 2020-02-04 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
459–768（310 aa）
|
Not recorded | SO4 SULFATE ION × 3 EVL N-ethyl-2-[[4-[[3-methoxy-4-[4-(4-methylpiperazin-1-yl)piperidin-1-yl]phenyl]amino]-1,3,5-triazin-2-yl]amino]benzenesulfonamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 8.5；296 K；Tris, Ammonium sulfate, PEG 8000
|
Resolution 2.98 Å R-free 0.251 |
| 6V6Q Crystal Structure of Monophosphorylated FGF Receptor 2 isoform IIIb with PTR657 Deposited 2019-12-05 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
413–821（409 aa）
Chain B
413–821（409 aa）
|
Mutation：Y467F,Y562F,Y576F,Y587F,Y589F,Y609F,Y617F,Y658F,Y734F Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y467F,Y562F,Y576F,Y587F,Y589F,Y609F,Y617F,Y658F,Y734F Non-standard monomer：Yes (specific site not provided by mmCIF) | ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.6；293 K；160mM TMAO, 20% PEG 2000, 100mM Tris pH 8.6
|
Resolution 2.46 Å R-free 0.239 |
| 6V6Q Crystal Structure of Monophosphorylated FGF Receptor 2 isoform IIIb with PTR657 Deposited 2019-12-05 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain C
413–821（409 aa）
Chain D
413–821（409 aa）
|
Mutation：Y467F,Y562F,Y576F,Y587F,Y589F,Y609F,Y617F,Y658F,Y734F Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y467F,Y562F,Y576F,Y587F,Y589F,Y609F,Y617F,Y658F,Y734F Non-standard monomer：Yes (specific site not provided by mmCIF) | ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.6；293 K；160mM TMAO, 20% PEG 2000, 100mM Tris pH 8.6
|
Resolution 2.46 Å R-free 0.239 |
| 7KIA Crystal structure of FGFR2 kinase domain gatekeeper mutant V564F in complex with covalent compound 19 Deposited 2020-10-23 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
461–768（308 aa）
Fragment：Kinase domain, residues 461-768
|
Mutation：V564F | WFD 1-[4-(4-{4-(4-methylpiperazin-1-yl)-6-[(3-methyl-1H-pyrazol-5-yl)amino]pyrimidin-2-yl}phenyl)piperidin-1-yl]prop-2-en-1-one × 1 FLC CITRATE ANION × 1 NA SODIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 4；298 K；12% w/v PEG 8000, 0.1M Sodium Citrate pH 4.0
|
Resolution 2.22 Å R-free 0.223 |
| 7KIA Crystal structure of FGFR2 kinase domain gatekeeper mutant V564F in complex with covalent compound 19 Deposited 2020-10-23 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
461–768（308 aa）
Fragment：Kinase domain, residues 461-768
|
Mutation：V564F | WFD 1-[4-(4-{4-(4-methylpiperazin-1-yl)-6-[(3-methyl-1H-pyrazol-5-yl)amino]pyrimidin-2-yl}phenyl)piperidin-1-yl]prop-2-en-1-one × 1 FLC CITRATE ANION × 1 NA SODIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 4；298 K；12% w/v PEG 8000, 0.1M Sodium Citrate pH 4.0
|
Resolution 2.22 Å R-free 0.223 |
| 7KIE Crystal structure of FGFR2 kinase domain gatekeeper mutant V564F in complex with covalent compound 3 Deposited 2020-10-23 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
461–768（308 aa）
Fragment：Kinase domain, residues 461-768
|
Mutation：V564F | WF7 N-{4-[(E)-2-{4-(4-methylpiperazin-1-yl)-6-[(5-methyl-1H-pyrazol-3-yl)amino]pyrimidin-2-yl}ethenyl]phenyl}prop-2-enamide × 1 FLC CITRATE ANION × 1 GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 4；298 K；15% w/v PEG 8000, 0.1M Sodium Citrate pH 4.0
|
Resolution 2.47 Å R-free 0.229 |
| 7KIE Crystal structure of FGFR2 kinase domain gatekeeper mutant V564F in complex with covalent compound 3 Deposited 2020-10-23 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
461–768（308 aa）
Fragment：Kinase domain, residues 461-768
|
Mutation：V564F | WF7 N-{4-[(E)-2-{4-(4-methylpiperazin-1-yl)-6-[(5-methyl-1H-pyrazol-3-yl)amino]pyrimidin-2-yl}ethenyl]phenyl}prop-2-enamide × 1 FLC CITRATE ANION × 1 GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 4；298 K；15% w/v PEG 8000, 0.1M Sodium Citrate pH 4.0
|
Resolution 2.47 Å R-free 0.229 |
| 7OZY FGFR2 kinase domain (residues 461-763) in complex with 38. Deposited 2021-06-29 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain AAA
465–763（299 aa）
|
Not recorded | 47I 4-[3-(4-piperazin-4-ium-1-ylphenyl)-1H-indazol-6-yl]phenol × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 7.6；291 K；25% w/v PEG 3350, 0.1 M ammonium sulfate, 0.1 M HEPES
|
Resolution 2.28 Å R-free 0.296 |
| 7OZY FGFR2 kinase domain (residues 461-763) in complex with 38. Deposited 2021-06-29 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain BBB
465–763（299 aa）
|
Not recorded | 47I 4-[3-(4-piperazin-4-ium-1-ylphenyl)-1H-indazol-6-yl]phenol × 1 SO4 SULFATE ION × 1 EDO 1,2-ETHANEDIOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 7.6；291 K；25% w/v PEG 3350, 0.1 M ammonium sulfate, 0.1 M HEPES
|
Resolution 2.28 Å R-free 0.296 |
| 8E1X FGFR2 kinase domain in complex with a Pyrazolo[1,5-a]pyrimidine analog (Compound 29) Deposited 2022-08-11 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
459–768（310 aa）
Chain B
459–768（310 aa）
|
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) | U9P (5M)-N-methyl-5-{(6M,8S)-5-{[(3S)-oxolan-3-yl]amino}-6-[1-(propan-2-yl)-1H-pyrazol-3-yl]pyrazolo[1,5-a]pyrimidin-3-yl}pyridine-3-carboxamide × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 5.2；293 K；0.1 M Sodium citrate pH 5.2; 28% w/w PEG 4,000; 0.2 M Ammonium acetate
|
Resolution 2.68 Å R-free 0.272 |
| 8H75 FGFR2 in complex with YJ001 Deposited 2022-10-19 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
347–656（310 aa）
Chain B
347–656（310 aa）
Chain C
347–656（310 aa）
Chain D
347–656（310 aa）
|
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) | KX0 Tinengotinib × 4 CL CHLORIDE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；0.2M (NH4)2SO4, 0.1M Bis-Tris pH6.0, 25% PEG3350.
|
Resolution 3.75 Å R-free 0.238 |
| 8STG Discovery and clinical validation of RLY-4008, the first highly selective FGFR2 inhibitor with activity across FGFR2 alterations and resistance mutations Deposited 2023-05-10 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
458–769（312 aa）
Fragment：kinase domain (UNP residues 458-769)
|
Not recorded | WCJ N-{4-[(5P)-4-amino-5-{3-fluoro-4-[(4-methylpyrimidin-2-yl)oxy]phenyl}-7-methyl-7H-pyrrolo[2,3-d]pyrimidin-6-yl]phenyl}-2-methylpropanamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；291.15 K；0.1 M Tris, pH 8, 18-20% w/v PEG8000
|
Resolution 3.79 Å R-free 0.311 |
| 8STG Discovery and clinical validation of RLY-4008, the first highly selective FGFR2 inhibitor with activity across FGFR2 alterations and resistance mutations Deposited 2023-05-10 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
458–769（312 aa）
Fragment：kinase domain (UNP residues 458-769)
|
Not recorded | WCJ N-{4-[(5P)-4-amino-5-{3-fluoro-4-[(4-methylpyrimidin-2-yl)oxy]phenyl}-7-methyl-7H-pyrrolo[2,3-d]pyrimidin-6-yl]phenyl}-2-methylpropanamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；291.15 K；0.1 M Tris, pH 8, 18-20% w/v PEG8000
|
Resolution 3.79 Å R-free 0.311 |
| 8SWE FGFR2 Kinase Domain Bound to Reversible Inhibitor Cmpd 3 Deposited 2023-05-18 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
458–768（311 aa）
|
Not recorded | GOL GLYCEROL × 1 GSH Glutathione × 1 WXQ N-{4-[4-amino-5-(4-methoxyphenyl)-7-methyl-7H-pyrrolo[2,3-d]pyrimidin-6-yl]phenyl}prop-2-enamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；291.15 K；27 % PEG 4000, 0.1 M Hepes pH7.5, 0.252 M Ammonium Sulfate, 0.05 M GSH GSSG
|
Resolution 2.24 Å R-free 0.250 |
| 8SWE FGFR2 Kinase Domain Bound to Reversible Inhibitor Cmpd 3 Deposited 2023-05-18 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
458–768（311 aa）
|
Not recorded | GOL GLYCEROL × 3 WXQ N-{4-[4-amino-5-(4-methoxyphenyl)-7-methyl-7H-pyrrolo[2,3-d]pyrimidin-6-yl]phenyl}prop-2-enamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；291.15 K；27 % PEG 4000, 0.1 M Hepes pH7.5, 0.252 M Ammonium Sulfate, 0.05 M GSH GSSG
|
Resolution 2.24 Å R-free 0.250 |
| 8U1F FGFR2 Kinase Domain Bound to Irreversible Inhibitor Cmpd 10 Deposited 2023-08-31 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
458–768（311 aa）
Chain B
458–768（311 aa）
|
Not recorded | GOL GLYCEROL × 1 UIM N-[4-(4-amino-7-methyl-5-{4-[(4-methylpyrimidin-2-yl)oxy]phenyl}-7H-pyrrolo[2,3-d]pyrimidin-6-yl)phenyl]-2-methylpropanamide × 2 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；291.15 K；0.1 M Tris pH 8, 18% PEG K
|
Resolution 3.33 Å R-free 0.295 |
| 8W2X TAS-120 covalent structure with FGFR2 Deposited 2024-02-21 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
458–768（311 aa）
|
Mutation：D650V | A1AFR 1-[(3S)-3-{4-amino-3-[(3,5-dimethoxyphenyl)ethynyl]-1H-pyrazolo[3,4-d]pyrimidin-1-yl}pyrrolidin-1-yl]propan-1-one × 1 GOL GLYCEROL × 1 SO4 SULFATE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.6；293 K；0.2 M Potassium sodium tartrate tetrahydrate 2.0 M Ammonium sulfate 0.1 M Sodium citrate 5.6
|
Resolution 2.98 Å R-free 0.237 |
| 8W2X TAS-120 covalent structure with FGFR2 Deposited 2024-02-21 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
458–768（311 aa）
|
Mutation：D650V | A1AFR 1-[(3S)-3-{4-amino-3-[(3,5-dimethoxyphenyl)ethynyl]-1H-pyrazolo[3,4-d]pyrimidin-1-yl}pyrrolidin-1-yl]propan-1-one × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.6；293 K；0.2 M Potassium sodium tartrate tetrahydrate 2.0 M Ammonium sulfate 0.1 M Sodium citrate 5.6
|
Resolution 2.98 Å R-free 0.237 |
| 8W38 TAS-120 covalent structure with FGFR2 molecular brake mutant Deposited 2024-02-22 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
458–768（311 aa）
|
Mutation：N549D, D650V | TZ0 1-[(3S)-3-{4-amino-3-[(3,5-dimethoxyphenyl)ethynyl]-1H-pyrazolo[3,4-d]pyrimidin-1-yl}pyrrolidin-1-yl]prop-2-en-1-one × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；25% PEG 3350, 0.2M LiSO4, 0.1M HEPES pH 7.5
|
Resolution 2.60 Å R-free 0.359 |
| 8W38 TAS-120 covalent structure with FGFR2 molecular brake mutant Deposited 2024-02-22 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
458–768（311 aa）
|
Mutation：N549D, D650V | TZ0 1-[(3S)-3-{4-amino-3-[(3,5-dimethoxyphenyl)ethynyl]-1H-pyrazolo[3,4-d]pyrimidin-1-yl}pyrrolidin-1-yl]prop-2-en-1-one × 1 SO4 SULFATE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；25% PEG 3350, 0.2M LiSO4, 0.1M HEPES pH 7.5
|
Resolution 2.60 Å R-free 0.359 |
| 8W38 TAS-120 covalent structure with FGFR2 molecular brake mutant Deposited 2024-02-22 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
458–768（311 aa）
|
Mutation：N549D, D650V | TZ0 1-[(3S)-3-{4-amino-3-[(3,5-dimethoxyphenyl)ethynyl]-1H-pyrazolo[3,4-d]pyrimidin-1-yl}pyrrolidin-1-yl]prop-2-en-1-one × 1 SO4 SULFATE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；25% PEG 3350, 0.2M LiSO4, 0.1M HEPES pH 7.5
|
Resolution 2.60 Å R-free 0.359 |
| 8W38 TAS-120 covalent structure with FGFR2 molecular brake mutant Deposited 2024-02-22 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain D
458–768（311 aa）
|
Mutation：N549D, D650V | TZ0 1-[(3S)-3-{4-amino-3-[(3,5-dimethoxyphenyl)ethynyl]-1H-pyrazolo[3,4-d]pyrimidin-1-yl}pyrrolidin-1-yl]prop-2-en-1-one × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；25% PEG 3350, 0.2M LiSO4, 0.1M HEPES pH 7.5
|
Resolution 2.60 Å R-free 0.359 |
| 8W3B TAS-120 covalent structure with FGFR2 molecular brake mutant Deposited 2024-02-22 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
458–768（311 aa）
|
Mutation：N549H, D650V | TZ0 1-[(3S)-3-{4-amino-3-[(3,5-dimethoxyphenyl)ethynyl]-1H-pyrazolo[3,4-d]pyrimidin-1-yl}pyrrolidin-1-yl]prop-2-en-1-one × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.2；291 K；0.2 M Lithium sulfate, 0.1 M HEPES 7.2, 25 % v/v PEG Smear Broad
|
Resolution 2.23 Å R-free 0.312 |
| 8W3B TAS-120 covalent structure with FGFR2 molecular brake mutant Deposited 2024-02-22 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
458–768（311 aa）
|
Mutation：N549H, D650V | TZ0 1-[(3S)-3-{4-amino-3-[(3,5-dimethoxyphenyl)ethynyl]-1H-pyrazolo[3,4-d]pyrimidin-1-yl}pyrrolidin-1-yl]prop-2-en-1-one × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.2；291 K；0.2 M Lithium sulfate, 0.1 M HEPES 7.2, 25 % v/v PEG Smear Broad
|
Resolution 2.23 Å R-free 0.312 |
| 8W3B TAS-120 covalent structure with FGFR2 molecular brake mutant Deposited 2024-02-22 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
458–768（311 aa）
|
Mutation：N549H, D650V | TZ0 1-[(3S)-3-{4-amino-3-[(3,5-dimethoxyphenyl)ethynyl]-1H-pyrazolo[3,4-d]pyrimidin-1-yl}pyrrolidin-1-yl]prop-2-en-1-one × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.2；291 K；0.2 M Lithium sulfate, 0.1 M HEPES 7.2, 25 % v/v PEG Smear Broad
|
Resolution 2.23 Å R-free 0.312 |
| 8W3B TAS-120 covalent structure with FGFR2 molecular brake mutant Deposited 2024-02-22 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain D
458–768（311 aa）
|
Mutation：N549H, D650V | TZ0 1-[(3S)-3-{4-amino-3-[(3,5-dimethoxyphenyl)ethynyl]-1H-pyrazolo[3,4-d]pyrimidin-1-yl}pyrrolidin-1-yl]prop-2-en-1-one × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.2；291 K；0.2 M Lithium sulfate, 0.1 M HEPES 7.2, 25 % v/v PEG Smear Broad
|
Resolution 2.23 Å R-free 0.312 |
| 8W3D TAS-120 covalent structure with FGFR2 molecular brake mutant Deposited 2024-02-22 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
458–768（311 aa）
|
Mutation：N549K, D650V | TZ0 1-[(3S)-3-{4-amino-3-[(3,5-dimethoxyphenyl)ethynyl]-1H-pyrazolo[3,4-d]pyrimidin-1-yl}pyrrolidin-1-yl]prop-2-en-1-one × 1 GOL GLYCEROL × 1 SO4 SULFATE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；291 K；0.2 M Lithium sulfate 0.1 M Bis-Tris 6.5 25 % w/v PEG 3350
|
Resolution 2.04 Å R-free 0.250 |
| 8W3D TAS-120 covalent structure with FGFR2 molecular brake mutant Deposited 2024-02-22 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
458–768（311 aa）
|
Mutation：N549K, D650V | TZ0 1-[(3S)-3-{4-amino-3-[(3,5-dimethoxyphenyl)ethynyl]-1H-pyrazolo[3,4-d]pyrimidin-1-yl}pyrrolidin-1-yl]prop-2-en-1-one × 1 GOL GLYCEROL × 2 SO4 SULFATE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；291 K；0.2 M Lithium sulfate 0.1 M Bis-Tris 6.5 25 % w/v PEG 3350
|
Resolution 2.04 Å R-free 0.250 |
| 8W3D TAS-120 covalent structure with FGFR2 molecular brake mutant Deposited 2024-02-22 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
458–768（311 aa）
|
Mutation：N549K, D650V | TZ0 1-[(3S)-3-{4-amino-3-[(3,5-dimethoxyphenyl)ethynyl]-1H-pyrazolo[3,4-d]pyrimidin-1-yl}pyrrolidin-1-yl]prop-2-en-1-one × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；291 K；0.2 M Lithium sulfate 0.1 M Bis-Tris 6.5 25 % w/v PEG 3350
|
Resolution 2.04 Å R-free 0.250 |
| 8W3D TAS-120 covalent structure with FGFR2 molecular brake mutant Deposited 2024-02-22 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain D
458–768（311 aa）
|
Mutation：N549K, D650V | TZ0 1-[(3S)-3-{4-amino-3-[(3,5-dimethoxyphenyl)ethynyl]-1H-pyrazolo[3,4-d]pyrimidin-1-yl}pyrrolidin-1-yl]prop-2-en-1-one × 1 GOL GLYCEROL × 1 SO4 SULFATE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；291 K；0.2 M Lithium sulfate 0.1 M Bis-Tris 6.5 25 % w/v PEG 3350
|
Resolution 2.04 Å R-free 0.250 |
| 9U3N Crystal structure of FGFR2 kinase domain gatekeeper mutant V564F in complex with compound LC-F2-01 Deposited 2025-03-18 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
458–768（311 aa）
|
Mutation：V564F | A1ENT ~{N}-[4-[4-azanyl-7-methyl-5-[2-(3-methylimidazo[4,5-b]pyridin-6-yl)ethynyl]pyrrolo[2,3-d]pyrimidin-6-yl]phenyl]prop-2-enamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；291 K；0.2M Sodium formate, 20% PEG3,3500+16% Glutaric acid, 0.16% Mellitic acid, 0.16% Oxalic acid, 0.16% Pimelic acid, 0.16% Sebacic acid,0.16% trans-Cinnamic acid, 0.02 M HEPES Na pH6.8
|
Resolution 3.25 Å R-free 0.342 |
| 9U3N Crystal structure of FGFR2 kinase domain gatekeeper mutant V564F in complex with compound LC-F2-01 Deposited 2025-03-18 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
458–768（311 aa）
|
Mutation：V564F | A1ENT ~{N}-[4-[4-azanyl-7-methyl-5-[2-(3-methylimidazo[4,5-b]pyridin-6-yl)ethynyl]pyrrolo[2,3-d]pyrimidin-6-yl]phenyl]prop-2-enamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；291 K；0.2M Sodium formate, 20% PEG3,3500+16% Glutaric acid, 0.16% Mellitic acid, 0.16% Oxalic acid, 0.16% Pimelic acid, 0.16% Sebacic acid,0.16% trans-Cinnamic acid, 0.02 M HEPES Na pH6.8
|
Resolution 3.25 Å R-free 0.342 |
| 9U7E FGFR2 kinase domain with a macrocyclic compound 8g Deposited 2025-03-24 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
465–768（304 aa）
Chain B
465–768（304 aa）
|
Not recorded | A1EOH (E)-4-methyl-17-(1-methyl-1H-pyrazol-4-yl)-7,10-dioxa-4-aza-1(3,6)-imidazo[1,2-b]pyridazina-2(3,5)-pyridinacyclodecaphan-3-one × 2 SO4 SULFATE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；293.15 K；16% PEG 3350, 100 mM (NH4)2SO4, 100 mM HEPES, pH 7.5
|
Resolution 2.20 Å R-free 0.312 |
| 9U7S FGFR2 kinase domain with a macrocyclic compound 8r Deposited 2025-03-25 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
465–768（304 aa）
Chain B
465–768（304 aa）
|
Not recorded | A1EOJ (E)-4-methyl-17-(1-(1-methylpiperidin-4-yl)-1H-pyrazol-4-yl)-7,10-dioxa-4-aza-1(3,6)-imidazo[1,2-b]pyridazina-2(1,3)-benzenacyclodecaphan-3-one × 2 SO4 SULFATE ION × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；293.15 K；18% PEG 3350, 100 mM (NH4)2SO4, 100 mM HEPES, pH 7.5
|
Resolution 1.99 Å R-free 0.225 |
| 9VLM The X-RAY co-crystal structure of human FGFR2 and covalent inhibitor 10a Deposited 2025-06-25 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
465–765（301 aa）
|
Not recorded | A1ESP ~{N}-[3-[2-[[3-[2-(dimethylamino)ethylsulfamoylmethyl]phenyl]amino]pyrimidin-4-yl]-1-methyl-indol-6-yl]propanamide × 1 GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；22% (w/v) PEG 8000, and 0.1 M Tris-HCl, pH 8.0
|
Resolution 2.26 Å R-free 0.254 |
| 9VLM The X-RAY co-crystal structure of human FGFR2 and covalent inhibitor 10a Deposited 2025-06-25 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
465–765（301 aa）
|
Not recorded | A1ESP ~{N}-[3-[2-[[3-[2-(dimethylamino)ethylsulfamoylmethyl]phenyl]amino]pyrimidin-4-yl]-1-methyl-indol-6-yl]propanamide × 1 GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；22% (w/v) PEG 8000, and 0.1 M Tris-HCl, pH 8.0
|
Resolution 2.26 Å R-free 0.254 |
60 other PDB entries and 118 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | FGFR2_HUMAN |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 14–324； UniProt 458–768 Author chain B； PDBConstruct 14–324； UniProt 458–768 Author chain C； PDBConstruct 14–324； UniProt 458–768 Author chain D； PDBConstruct 14–324； UniProt 458–768 |
