SAXSdb — 7ysu

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Klotho

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	Other combination Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 34–975	Not recorded	Fibroblast growth factor receptor 3 × 2 （P22607） Fibroblast growth factor 23 × 1 （Q9GZV9） ;2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid ; × 1 ZN ZINC ION × 1 CU COPPER (II) ION × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.20 Å

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 7YSU	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
5W21 Crystal Structure of a 1:1:1 FGF23-FGFR1c-aKlotho Ternary Complex Deposited 2017-06-05	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–981（981 aa） Fragment：ectodomain (UNP residues 1-981)	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 7 ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；22% PEG350 MME, 0.1 M Tris-HCl, pH 8.0, 1 mM reduced glutathione, 1 mM oxidized glutathione	Resolution 3.00 Å R-free 0.278
7YSH Cryo-EM Structure of FGF23-FGFR1c-aKlotho-HS Quaternary Complex Deposited 2022-08-12	Different construct Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 34–981（948 aa）	Not recorded	ZN ZINC ION × 1 CU COPPER (II) ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.74 Å
7YSW Cryo-EM Structure of FGF23-FGFR4-aKlotho-HS Quaternary Complex Deposited 2022-08-13	Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 34–975（942 aa）	Not recorded	CU COPPER (II) ION × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.03 Å
8TOH Cryo-EM structure of monomeric alpha-Klotho Deposited 2023-08-03	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 34–981（948 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；25mM HEPES pH7.5, 300mM NaCl, 1mM TCEP cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.29 Å
8UF8 Cryo-EM structure of alpha-Klotho Deposited 2023-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–1012（1012 aa） Chain B 1–1012（1012 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；20mM HEPES pH7.5, 150mM NaCl, 1mM DTT cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.50 Å

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	KLOT_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–942； UniProt 34–975

Fibroblast growth factor receptor 3

Homo sapiens

UniProt P22607

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Other combination Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain C； UniProt 148–358 Chain E； UniProt 148–358	Not recorded	Klotho × 1 （Q9UEF7） Fibroblast growth factor 23 × 1 （Q9GZV9） ;2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid ; × 1 ZN ZINC ION × 1 CU COPPER (II) ION × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.20 Å

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 7YSU	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1RY7 Crystal Structure of the 3 Ig form of FGFR3c in complex with FGF1 Deposited 2003-12-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 33–365（333 aa） Fragment：FGFR-3c	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；Peg 4000, glycerol, MPD, cadmium chloride, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.20 Å R-free 0.341
2LZL FGFR3tm Deposited 2012-10-04	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 357–399（43 aa） Fragment：UNP residues 357-399 Chain B 357–399（43 aa） Fragment：UNP residues 357-399	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.7；313 K；Ionic strength (raw mmCIF value) 50；Pressure ambient NMR sample composition 0.75 mM [U-99% 13C; U-99% 15N] FGFR3tm, 0.75 mM FGFR3tm, 88 mM [U-99% 2H] DPC, 10 mM [U-99% 2H] SDS, 0.3 mM sodium azide, 6 mM TCEP, 5 mM citric acid, 15 mM Na2HPO4, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
4K33 Crystal Structure of FGF Receptor 3 (FGFR3) Kinase Domain Harboring the K650E Mutation, a Gain-of-Function Mutation Responsible for Thanatophoric Dysplasia Type II and Spermatocytic Seminoma Deposited 2013-04-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 449–759（311 aa） Fragment：Human FGF Receptor 3 Kinase Domain	Mutation：C482A, C582S, K650E	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, 19% PEG 4000, 4% C4H10O2, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.34 Å R-free 0.228
6LVM Crystal structure of FGFR3 in complex with pyrimidine derivative Deposited 2020-02-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 472–759（288 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	EVR 2-[[5-[2-(3,5-dimethoxyphenyl)ethyl]-2-[[3-methoxy-4-[4-(4-methylpiperazin-1-yl)piperidin-1-yl]phenyl]amino]pyrimidin-4-yl]amino]-N-ethyl-benzenesulfonamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；296 K；Citric Acid, PEG 8000	Resolution 2.53 Å R-free 0.279
6PNX Crystal Structure of an Asymmetric Dimer of FGF Receptor 3 Kinases Trapped in A-loop Tyrosine Transphosphorylation Reaction Deposited 2019-07-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 451–759（309 aa） Chain B 451–759（309 aa）	Mutation：C482A, C582S, R669E Mutation：C482A, C582S, R669E	ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 2 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；292 K；0.1 M Hepes, pH 7.5, and 1.8 M (NH4)2SO4	Resolution 2.20 Å R-free 0.230
7DHL Crystal structure of FGFR3 in complex with pyrimidine derivative Deposited 2020-11-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 472–759（288 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	H6X 5-[2-(3,5-dimethoxyphenyl)ethyl]-N-[3-methoxy-4-[4-(4-methylpiperazin-1-yl)piperidin-1-yl]phenyl]pyrimidin-2-amine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；293 K；Citric Acid, Ammonium dihydrogen phosphate, PEG 3350	Resolution 2.57 Å R-free 0.254
8UDT The X-RAY co-crystal structure of human FGFR3 and KIN-3248 Deposited 2023-09-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 455–756（302 aa） Fragment：kinase domain	Mutation：residues 572-585 replaced by Ser-Gly	MLT D-MALATE × 2 WGF 3-[(1-cyclopropyl-4,6-difluoro-1H-benzimidazol-5-yl)ethynyl]-1-[(3R,5R)-5-(methoxymethyl)-1-propanoylpyrrolidin-3-yl]-5-(methylamino)-1H-pyrazole-4-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.20 M DL-Malic acid pH 5.00, 18.00 % (w/v) PEG 4000	Resolution 2.83 Å R-free 0.274
8UDT The X-RAY co-crystal structure of human FGFR3 and KIN-3248 Deposited 2023-09-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 455–756（302 aa） Fragment：kinase domain	Mutation：residues 572-585 replaced by Ser-Gly	WGF 3-[(1-cyclopropyl-4,6-difluoro-1H-benzimidazol-5-yl)ethynyl]-1-[(3R,5R)-5-(methoxymethyl)-1-propanoylpyrrolidin-3-yl]-5-(methylamino)-1H-pyrazole-4-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.20 M DL-Malic acid pH 5.00, 18.00 % (w/v) PEG 4000	Resolution 2.83 Å R-free 0.274
8UDT The X-RAY co-crystal structure of human FGFR3 and KIN-3248 Deposited 2023-09-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 455–756（302 aa） Fragment：kinase domain	Mutation：residues 572-585 replaced by Ser-Gly	WGF 3-[(1-cyclopropyl-4,6-difluoro-1H-benzimidazol-5-yl)ethynyl]-1-[(3R,5R)-5-(methoxymethyl)-1-propanoylpyrrolidin-3-yl]-5-(methylamino)-1H-pyrazole-4-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.20 M DL-Malic acid pH 5.00, 18.00 % (w/v) PEG 4000	Resolution 2.83 Å R-free 0.274
8UDU The X-RAY co-crystal structure of human FGFR3 and Compound 17 Deposited 2023-09-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 455–756（302 aa） Fragment：kinase domain	Mutation：residues 572-585 replaced by Ser-Gly	CL CHLORIDE ION × 1 WIQ 3-[(6-chloro-1-cyclopropyl-1H-benzimidazol-5-yl)ethynyl]-1-[(3S,5S)-5-(methoxymethyl)-1-(prop-2-enoyl)pyrrolidin-3-yl]-5-(methylamino)-1H-pyrazole-4-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.10 M Magnesium Chloride, 0.10 M TRIS/HCl pH 8.10, 0.20 M Sodium Chloride, 20.00 % (w/v) PEG 3350	Resolution 1.74 Å R-free 0.256
8UDU The X-RAY co-crystal structure of human FGFR3 and Compound 17 Deposited 2023-09-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 455–756（302 aa） Fragment：kinase domain	Mutation：residues 572-585 replaced by Ser-Gly	CL CHLORIDE ION × 1 WIQ 3-[(6-chloro-1-cyclopropyl-1H-benzimidazol-5-yl)ethynyl]-1-[(3S,5S)-5-(methoxymethyl)-1-(prop-2-enoyl)pyrrolidin-3-yl]-5-(methylamino)-1H-pyrazole-4-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.10 M Magnesium Chloride, 0.10 M TRIS/HCl pH 8.10, 0.20 M Sodium Chloride, 20.00 % (w/v) PEG 3350	Resolution 1.74 Å R-free 0.256
8UDV The X-RAY co-crystal structure of human FGFR3 V555M and Compound 17 Deposited 2023-09-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 455–756（302 aa） Fragment：kinase domain	Mutation：V555M and residues 572-585 (Uniprot numbering) replaced by Ser-Gly	SO4 SULFATE ION × 3 WIQ 3-[(6-chloro-1-cyclopropyl-1H-benzimidazol-5-yl)ethynyl]-1-[(3S,5S)-5-(methoxymethyl)-1-(prop-2-enoyl)pyrrolidin-3-yl]-5-(methylamino)-1H-pyrazole-4-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.10 M BIS-TRIS/HCl pH 6.50, 0.20 M (NH4)2SO4, 25.00 % (w/v) PEG 3350	Resolution 2.35 Å R-free 0.261
8UDV The X-RAY co-crystal structure of human FGFR3 V555M and Compound 17 Deposited 2023-09-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 455–756（302 aa） Fragment：kinase domain	Mutation：V555M and residues 572-585 (Uniprot numbering) replaced by Ser-Gly	SO4 SULFATE ION × 2 WIQ 3-[(6-chloro-1-cyclopropyl-1H-benzimidazol-5-yl)ethynyl]-1-[(3S,5S)-5-(methoxymethyl)-1-(prop-2-enoyl)pyrrolidin-3-yl]-5-(methylamino)-1H-pyrazole-4-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.10 M BIS-TRIS/HCl pH 6.50, 0.20 M (NH4)2SO4, 25.00 % (w/v) PEG 3350	Resolution 2.35 Å R-free 0.261
8UDV The X-RAY co-crystal structure of human FGFR3 V555M and Compound 17 Deposited 2023-09-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 455–756（302 aa） Fragment：kinase domain	Mutation：V555M and residues 572-585 (Uniprot numbering) replaced by Ser-Gly	SO4 SULFATE ION × 2 WIQ 3-[(6-chloro-1-cyclopropyl-1H-benzimidazol-5-yl)ethynyl]-1-[(3S,5S)-5-(methoxymethyl)-1-(prop-2-enoyl)pyrrolidin-3-yl]-5-(methylamino)-1H-pyrazole-4-carboxamide × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.10 M BIS-TRIS/HCl pH 6.50, 0.20 M (NH4)2SO4, 25.00 % (w/v) PEG 3350	Resolution 2.35 Å R-free 0.261
9CD7 FGFR3 Kinase Domain with Inhibitor TYRA-300 Deposited 2024-06-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 448–759（312 aa）	Mutation：C482A, C582S, K650E	A1AV2 (3P)-5-[(1R)-1-(3,5-dichloropyridin-4-yl)ethoxy]-3-{6-[6-(methanesulfonyl)-2,6-diazaspiro[3.3]heptan-2-yl]pyridin-3-yl}-1H-indazole × 1 GOL GLYCEROL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.25；291 K；17% PEG Smear Medium 10% Tacsimate pH 5.25 0.2M Ammonium Sulfate	Resolution 2.53 Å R-free 0.267
9CD7 FGFR3 Kinase Domain with Inhibitor TYRA-300 Deposited 2024-06-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 448–759（312 aa）	Mutation：C482A, C582S, K650E	A1AV2 (3P)-5-[(1R)-1-(3,5-dichloropyridin-4-yl)ethoxy]-3-{6-[6-(methanesulfonyl)-2,6-diazaspiro[3.3]heptan-2-yl]pyridin-3-yl}-1H-indazole × 1 GOL GLYCEROL × 6 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.25；291 K；17% PEG Smear Medium 10% Tacsimate pH 5.25 0.2M Ammonium Sulfate	Resolution 2.53 Å R-free 0.267
9CD7 FGFR3 Kinase Domain with Inhibitor TYRA-300 Deposited 2024-06-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 448–759（312 aa）	Mutation：C482A, C582S, K650E	A1AV2 (3P)-5-[(1R)-1-(3,5-dichloropyridin-4-yl)ethoxy]-3-{6-[6-(methanesulfonyl)-2,6-diazaspiro[3.3]heptan-2-yl]pyridin-3-yl}-1H-indazole × 1 GOL GLYCEROL × 6 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.25；291 K；17% PEG Smear Medium 10% Tacsimate pH 5.25 0.2M Ammonium Sulfate	Resolution 2.53 Å R-free 0.267
9D1X Crystal structure of FGFR3 bound to indazole inhibitor Deposited 2024-08-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 455–756（302 aa） Fragment：kinase domain	Mutation：P572S, P573G	A1A6M (3P)-N-(2,6-dimethylphenyl)-6-methoxy-3-(1-methyl-1H-pyrazol-4-yl)-1H-indazole-5-carboxamide × 1 CL CHLORIDE ION × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.1；293 K；0.2 M magnesium chloride, 0.3 M sodium chloride, 23% (w/v) PEG 3350, 0.1 M Tris-HCl pH 8.1	Resolution 1.60 Å R-free 0.190
9EKO A chimeric hybrid protein fused with the FGFR3 Transmembrane Domain Deposited 2024-12-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 371–399（29 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.90 Å R-free 0.287
9KFU Human FGFR3 in complex with inhibitor F1 Deposited 2024-11-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 448–756（309 aa）	Not recorded	A1L5T (7~{S})-2-azanyl-7-(4-fluorophenyl)-6,7-dihydro-4~{H}-[1,3]thiazolo[4,5-b]pyridin-5-one × 1 SO4 SULFATE ION × 4 CO COBALT (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293.15 K；25mM HEPES pH7.5, 1.8-2.0 M LiSO4, 10 Mm CoCl2	Resolution 1.40 Å R-free 0.251
9VM9 Crystal structure of FGFR3 in complex with 10s Deposited 2025-06-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 455–756（302 aa）	Not recorded	A1ESW ~{N}-[1-methyl-3-[2-[[5-methyl-1-(2-morpholin-4-ylethyl)pyrazol-4-yl]amino]pyrimidin-4-yl]indol-6-yl]propanamide × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；25% (w/v) PEG 3350, 0.2 M MgCl2, and 0.1 M HEPES, pH 7.5	Resolution 2.65 Å R-free 0.312
9VM9 Crystal structure of FGFR3 in complex with 10s Deposited 2025-06-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 455–756（302 aa）	Not recorded	A1ESW ~{N}-[1-methyl-3-[2-[[5-methyl-1-(2-morpholin-4-ylethyl)pyrazol-4-yl]amino]pyrimidin-4-yl]indol-6-yl]propanamide × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；25% (w/v) PEG 3350, 0.2 M MgCl2, and 0.1 M HEPES, pH 7.5	Resolution 2.65 Å R-free 0.312
9VM9 Crystal structure of FGFR3 in complex with 10s Deposited 2025-06-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 455–756（302 aa）	Not recorded	A1ESW ~{N}-[1-methyl-3-[2-[[5-methyl-1-(2-morpholin-4-ylethyl)pyrazol-4-yl]amino]pyrimidin-4-yl]indol-6-yl]propanamide × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；25% (w/v) PEG 3350, 0.2 M MgCl2, and 0.1 M HEPES, pH 7.5	Resolution 2.65 Å R-free 0.312
9VM9 Crystal structure of FGFR3 in complex with 10s Deposited 2025-06-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 455–756（302 aa）	Not recorded	A1ESW ~{N}-[1-methyl-3-[2-[[5-methyl-1-(2-morpholin-4-ylethyl)pyrazol-4-yl]amino]pyrimidin-4-yl]indol-6-yl]propanamide × 1 MG MAGNESIUM ION × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；25% (w/v) PEG 3350, 0.2 M MgCl2, and 0.1 M HEPES, pH 7.5	Resolution 2.65 Å R-free 0.312
9VMB The X-RAY co-crystal structure of human FGFR3 and Compound 10t Deposited 2025-06-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 455–756（302 aa）	Not recorded	A1ESX ~{N}-[1-methyl-3-[2-[[3-methyl-1-(2-morpholin-4-ylethyl)pyrazol-4-yl]amino]pyrimidin-4-yl]indol-6-yl]propanamide × 1 MG MAGNESIUM ION × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；25% (w/v) PEG 3350, 0.2 M MgCl2, and 0.1 M HEPES, pH 7.5	Resolution 1.97 Å R-free 0.237
9VMB The X-RAY co-crystal structure of human FGFR3 and Compound 10t Deposited 2025-06-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 455–756（302 aa）	Not recorded	A1ESX ~{N}-[1-methyl-3-[2-[[3-methyl-1-(2-morpholin-4-ylethyl)pyrazol-4-yl]amino]pyrimidin-4-yl]indol-6-yl]propanamide × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；25% (w/v) PEG 3350, 0.2 M MgCl2, and 0.1 M HEPES, pH 7.5	Resolution 1.97 Å R-free 0.237
9VMB The X-RAY co-crystal structure of human FGFR3 and Compound 10t Deposited 2025-06-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 455–756（302 aa）	Not recorded	A1ESX ~{N}-[1-methyl-3-[2-[[3-methyl-1-(2-morpholin-4-ylethyl)pyrazol-4-yl]amino]pyrimidin-4-yl]indol-6-yl]propanamide × 1 MG MAGNESIUM ION × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；25% (w/v) PEG 3350, 0.2 M MgCl2, and 0.1 M HEPES, pH 7.5	Resolution 1.97 Å R-free 0.237
9VMB The X-RAY co-crystal structure of human FGFR3 and Compound 10t Deposited 2025-06-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 455–756（302 aa）	Not recorded	A1ESX ~{N}-[1-methyl-3-[2-[[3-methyl-1-(2-morpholin-4-ylethyl)pyrazol-4-yl]amino]pyrimidin-4-yl]indol-6-yl]propanamide × 1 MG MAGNESIUM ION × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；25% (w/v) PEG 3350, 0.2 M MgCl2, and 0.1 M HEPES, pH 7.5	Resolution 1.97 Å R-free 0.237

15 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	FGFR3_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–211； UniProt 148–358 Author chain E； PDBConstruct 1–211； UniProt 148–358

Fibroblast growth factor 23

Homo sapiens

UniProt Q9GZV9

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Other combination Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain B； UniProt 25–203	Not recorded	Klotho × 1 （Q9UEF7） Fibroblast growth factor receptor 3 × 2 （P22607） ;2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid ; × 1 ZN ZINC ION × 1 CU COPPER (II) ION × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.20 Å

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 7YSU	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2P39 Crystal structure of human FGF23 Deposited 2007-03-08	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 25–179（155 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；100 mM Tris-HCl, 1.0 M (NH4)2SO4, 10 mM [Co(NH3)6]Cl3, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.50 Å R-free 0.214
5W21 Crystal Structure of a 1:1:1 FGF23-FGFR1c-aKlotho Ternary Complex Deposited 2017-06-05	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 25–204（180 aa） Fragment：UNP residues 25-204	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 7 ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；22% PEG350 MME, 0.1 M Tris-HCl, pH 8.0, 1 mM reduced glutathione, 1 mM oxidized glutathione	Resolution 3.00 Å R-free 0.278
6S22 Crystal structure of the TgGalNAc-T3 in complex with UDP, manganese and FGF23c Deposited 2019-06-20	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 170–181（12 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 14 SO4 SULFATE ION × 1 UDP URIDINE-5'-DIPHOSPHATE × 1 MN MANGANESE (II) ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 GOL GLYCEROL × 1 NGA 2-acetamido-2-deoxy-beta-D-galactopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；Morpheus precipitant mix 4, nitrate phosphate buffer and Morpheus buffer System 1	Resolution 1.96 Å R-free 0.216
7YSH Cryo-EM Structure of FGF23-FGFR1c-aKlotho-HS Quaternary Complex Deposited 2022-08-12	Different construct Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 25–251（227 aa）	Not recorded	ZN ZINC ION × 1 CU COPPER (II) ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.74 Å
7YSW Cryo-EM Structure of FGF23-FGFR4-aKlotho-HS Quaternary Complex Deposited 2022-08-13	Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 25–203（179 aa）	Not recorded	CU COPPER (II) ION × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.03 Å

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	FGF23_HUMAN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain B； PDBConstruct 1–179； UniProt 25–203

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	7ysu
Deposition date deposition_date	2022-08-13
Structure title title	Cryo-EM Structure of FGF23-FGFR3c-aKlotho-HS Quaternary Complex
Keywords keywords	FGF hormones, FGF Receptor, Klotho Co-Receptor, Heparan Sulfate Glycosaminoglycans, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	43.65 Å
Radius of gyration Rg (electron density) rg_electron	43.26 Å
Forward intensity I(0) i0	462312000.00
Molecular weight molecular_weight	176190.0 kDa
Excluded volume excluded_volume	219820 Å³
Envelope volume envelope_volume	301540 Å³
Hydration-shell volume shell_volume	57993 Å³
Envelope diameter envelope_diameter	141.7 Å
Shell Rg shell_rg	48.38 Å
Envelope Rg envelope_rg	42.32 Å
Shape Rg shape_rg	43.26 Å
Total Rg total_rg	43.51 Å
Total atoms total_atoms	12430
Residues n_residues	1521
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	140.8 Å
Rg (real space) rg_real	43.63 Å
Rg uncertainty (real space) rg_real_error	1.19 Å
I(0) (real space) i0_real	4.6230e+08
I(0) uncertainty (real space) i0_real_error	8.7750e+06
Rg (reciprocal space) rg_reciprocal	43.65 Å
I(0) (reciprocal space) i0_reciprocal	462300000.0000
Solution quality estimate total_estimate	0.8306
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	43.0 Å
Skewness Skewness skewness	0.210
Kurtosis Kurtosis kurtosis	-0.687
Angular range angular_range	— – 0.1800 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	53770000.0000
Real-space data points n_real_points	37
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.938; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	Klotho
Molecular weight formula_weight	108404.9 kDa
EC 编号 ec_number	3.2.1.31
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	12430

EPGDGAQTWARFSRPPAPEAAGLFQGTFPDGFLWAVGSAAYQTEGGWQQHGKGASIWDTFTHHPLAPPGDSRNASLPLGAPSPLQPATGDVASDSYNNVFRDTEALRELGVTHYRFSISWARVLPNGSAGVPNREGLRYYRRLLERLRELGVQPVVTLYHWDLPQRLQDAYGGWANRALADHFRDYAELCFRHFGGQVKYWITIDNPYVVAWHGYATGRLAPGIRGSPRLGYLVAHNLLLAHAKVWHLYNTSFRPTQGGQVSIALSSHWINPRRMTDHSIKECQKSLDFVLGWFAKPVFIDGDYPESMKNNLSSILPDFTESEKKFIKGTADFFALCFGPTLSFQLLDPHMKFRQLESPNLRQLLSWIDLEFNHPQIFIVENGWFVSGTTKRDDAKYMYYLKKFIMETLKAIKLDGVDVIGYTAWSLMDGFEWHRGYSIRRGLFYVDFLSQDKMLLPKSSALFYQKLIEKNGFPPLPENQPLEGTFPCDFAWGVVDNYIQVDTTLSQFTDLNVYLWDVHHSKRLIKVDGVVTKKRKSYCVDFAAIQPQIALLQEMHVTHFRFSLDWALILPLGNQSQVNHTILQYYRCMASELVRVNITPVVALWQPMAPNQGLPRLLARQGAWENPYTALAFAEYARLCFQELGHHVKLWITMNEPYTRNMTYSAGHNLLKAHALAWHVYNEKFRHAQNGKISIALQADWIEPACPFSQKDKEVAERVLEFDIGWLAEPIFGSGDYPWVMRDWLNQRNNFLLPYFTEDEKKLIQGTFDFLALSHYTTILVDSEKEDPIKYNDYLEVQEMTDITWLNSPSQVAVVPWGLRKVLNWLKFKYGDLPMYIISNGIDDGLHAEDDQLRVYYMQNYINEALKAHILDGINLCGYFAYSFNDRTAPRFGLYRYAADQFEPKASMKHYRKIIDSNGFPGPETLERFCPEEFTVCTECSF

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Homo sapiens

Entity 2 Entity 2 polymer

Description description	Fibroblast growth factor receptor 3
Molecular weight formula_weight	23358.4 kDa
EC 编号 ec_number	2.7.10.1
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,E

TGAPYWTRPERMDKKLLAVPAANTVRFRCPAAGNPTPSISWLKNGREFRGEHRIGGIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGSIRQTYTLDVLERSPHRPILQAGLPANQTAVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKVGPDGTPYVTVLKTAGANTTDKELEVLSLHNVTFEDAGEYTCLAGNSIGFSHHSAWLVVLP

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Homo sapiens

Entity 3 Entity 3 polymer

Description description	Fibroblast growth factor 23
Molecular weight formula_weight	20450.1 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

YPNASPLLGSSWGGLIHLYTATARNSYHLQIHKNGHVDGAPHQTIYSALMIRSEDAGFVVITGVMSRRYLCMDFRGNIFGSHYFDPENCRFQHQTLENGYDVYHSPQYHFLVSLGRAKRAFLPGMNPPPYSQFLSRRNEIPLIHFNTPIPRQHTQSAEDDSERDPLNVLKPRARMTPAP

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 4 Entity 4 branched

Description description	;2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid ;
Molecular weight formula_weight	2905.4 kDa
Source method src_method	man
Copy count entity_count	1

Entity 5 Entity 5 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 non-polymer

Description description	COPPER (II) ION
Molecular weight formula_weight	63.5 kDa
Source method src_method	syn
Copy count entity_count	1

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	7ysuA01
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	80 — Glycosidases

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	3.20 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	291540

fit	/app/data/saxs_computation/ys/7ysu/7ysu.fit
pddf	/app/data/pr_computation/ys/7ysu/7ysu.pr.out
profile	/app/data/saxs_computation/ys/7ysu/7ysu.dat

Cryo-EM Structure of FGF23-FGFR3c-aKlotho-HS Quaternary Complex

1. Protein Identity and Related Structures Protein Identity & Related Structures

Klotho

State in the Current Structure

Other States of the Same Protein in the Database

Fibroblast growth factor receptor 3

State in the Current Structure

Other States of the Same Protein in the Database

Fibroblast growth factor 23

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 branched

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)