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4hck

HUMAN HCK SH3 DOMAIN, NMR, 25 STRUCTURES

Method: SOLUTION NMR Dmax: 38.1 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

HEMATOPOIETIC CELL KINASE

Homo sapiens

UniProt P08631

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 72–143 Fragment：SH3 DOMAIN No other associated polymer SOLUTION NMR NMR measurement conditions：pH 6.25；298 K Resolution not provided

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 4HCK Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1AD5 SRC FAMILY KINASE HCK-AMP-PNP COMPLEX Deposited 1997-02-20 Different construct Different mutation/modification 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 79–526（448 aa） Fragment：SH3-SH2-KINASE-REGULATORY TAIL
Non-standard monomer：Yes (specific site not provided by mmCIF) CA CALCIUM ION × 2 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions vapor diffusion - hanging drop and seeding；pH 6.5；292 K；HANGING DROPS (1UL) OF 50MG/ML PROTEIN AND 10MM AMP-PNP WERE MIXED WITH EQUAL VOLUMES OF RESERVOIR BUFFER CONTAINING 150 MM CALCIUM ACETATE, 100MM CACODYLATE (PH 6.5), 7% PEG 8000 AND 16% V/V ETHYLENE GLYCOL. THE MIXED DROPS WERE THEN SEEDED AND STORED AT 19 DEGREES C., vapor diffusion - hanging drop and seeding, temperature 292K
Resolution 2.60 Å R-free 0.307
1AD5 SRC FAMILY KINASE HCK-AMP-PNP COMPLEX Deposited 1997-02-20 Different construct Different mutation/modification 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 79–526（448 aa） Fragment：SH3-SH2-KINASE-REGULATORY TAIL
Non-standard monomer：Yes (specific site not provided by mmCIF) CA CALCIUM ION × 2 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions vapor diffusion - hanging drop and seeding；pH 6.5；292 K；HANGING DROPS (1UL) OF 50MG/ML PROTEIN AND 10MM AMP-PNP WERE MIXED WITH EQUAL VOLUMES OF RESERVOIR BUFFER CONTAINING 150 MM CALCIUM ACETATE, 100MM CACODYLATE (PH 6.5), 7% PEG 8000 AND 16% V/V ETHYLENE GLYCOL. THE MIXED DROPS WERE THEN SEEDED AND STORED AT 19 DEGREES C., vapor diffusion - hanging drop and seeding, temperature 292K
Resolution 2.60 Å R-free 0.307
1BU1 SRC FAMILY KINASE HCK SH3 DOMAIN Deposited 1998-09-09 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 81–137（57 aa） Fragment：SH3
Chain B 81–137（57 aa） Fragment：SH3
Chain C 81–137（57 aa） Fragment：SH3
Chain D 81–137（57 aa） Fragment：SH3
Chain E 81–137（57 aa） Fragment：SH3
Chain F 81–137（57 aa） Fragment：SH3
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9.3；294 K；HANGING DROPS (2UL) OF 4.3MG/ML PROTEIN WERE MIXED WITH EQUAL VOLUMES OF RESERVOIR BUFFER CONTAINING 3.7 M SODIUM FORMATE, 2% PEG 3000, 100 MM BICINE (PH 9.3). THE MIXED DROPS WERE STORED AT 21 DEGREES, vapor diffusion - hanging drop, temperature 294K
Resolution 2.60 Å R-free 0.297
1QCF CRYSTAL STRUCTURE OF HCK IN COMPLEX WITH A SRC FAMILY-SELECTIVE TYROSINE KINASE INHIBITOR Deposited 1999-05-04 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：SH3-SH2-KINASE-HIGH AFFINITY TAIL
Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF) PP1 1-TER-BUTYL-3-P-TOLYL-1H-PYRAZOLO[3,4-D]PYRIMIDIN-4-YLAMINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；PEG 10000, DIMETHYL SULFOXIDE, N-(2-HYDROXYETHYL)PIPERAZINE-N-(2- ETHANESULFONIC ACID), pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.00 Å R-free 0.257
2C0I Src family kinase Hck with bound inhibitor A-420983 Deposited 2005-09-03 Different construct Different mutation/modification 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 80–525（446 aa） Fragment：SH3-SH2-SH1, RESIDUES 80-525
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) L1G N-(4-{4-AMINO-1-[4-(4-METHYLPIPERAZIN-1-YL)-TRANS-CYCLOHEXYL]-1H-PYRAZOLO[3,4-D]PYRIMIDIN-3-YL}-2-METHOXYPHENYL)-1-METHYL-1H-INDOLE-2-CARBOXAMIDE × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；HCK (10 MG/ML IN 150 MM NACL, 20 MM TRIS.HCL PH 8.0) WAS MIXED WITH A-420983 [100 MM STOCK SOLUTION OF THE BIS-MALEIC ACID SALT IN DMSO) TO GIVE A FINAL A-420983 CONCENTRATION OF 1 MM. HCK/A-420983 WAS THEN MIXED WITH RESERVOIR SOLUTION (12% PEG 6000, 3% 1, 5-DIAMINOPENTANE, 20% GLYCEROL, 200 MM CA(OAC)2, 100 MM TRIS.HCL PH 8.0) AND EQUILBRATED AGAINST THE RESERVOIR SOLUTION BY VAPOR DIFFUSION (SITTING DROPS) AT 277 K.
Resolution 2.30 Å R-free 0.274
2C0I Src family kinase Hck with bound inhibitor A-420983 Deposited 2005-09-03 Different construct Different mutation/modification 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 80–525（446 aa） Fragment：SH3-SH2-SH1, RESIDUES 80-525
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) L1G N-(4-{4-AMINO-1-[4-(4-METHYLPIPERAZIN-1-YL)-TRANS-CYCLOHEXYL]-1H-PYRAZOLO[3,4-D]PYRIMIDIN-3-YL}-2-METHOXYPHENYL)-1-METHYL-1H-INDOLE-2-CARBOXAMIDE × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；HCK (10 MG/ML IN 150 MM NACL, 20 MM TRIS.HCL PH 8.0) WAS MIXED WITH A-420983 [100 MM STOCK SOLUTION OF THE BIS-MALEIC ACID SALT IN DMSO) TO GIVE A FINAL A-420983 CONCENTRATION OF 1 MM. HCK/A-420983 WAS THEN MIXED WITH RESERVOIR SOLUTION (12% PEG 6000, 3% 1, 5-DIAMINOPENTANE, 20% GLYCEROL, 200 MM CA(OAC)2, 100 MM TRIS.HCL PH 8.0) AND EQUILBRATED AGAINST THE RESERVOIR SOLUTION BY VAPOR DIFFUSION (SITTING DROPS) AT 277 K.
Resolution 2.30 Å R-free 0.274
2C0O Src family kinase Hck with bound inhibitor A-770041 Deposited 2005-09-06 Different construct Different mutation/modification 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 80–525（446 aa） Fragment：SH3-SH2-SH1, RESIDUES 80-525
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) L2G N-(4-{1-[4-(4-ACETYLPIPERAZIN-1-YL)-TRANS-CYCLOHEXYL]-4-AMINO-1H-PYRAZOLO[3,4-D]PYRIMIDIN-3-YL}-2-METHOXYPHENYL)-1-METHYL-1H-INDOLE-2-CARBOXAMIDE × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；HCK (10 MG/ML IN 150 MM NACL, 20 MM TRIS.HCL PH 8.0) WAS MIXED WITH A-770041 [100 MM STOCK SOLUTION IN DMSO) TO GIVE A FINAL A-770041 CONCENTRATION OF 1 MM. HCK/A-770041 WAS THEN MIXED WITH RESERVOIR SOLUTION (12% PEG 6000, 3% 1,5-DIAMINOPENTANE, 20% GLYCEROL, 200 MM CA(OAC)2, 100 MM TRIS.HCL PH 8.0) AND EQUILBRATED AGAINST THE RESERVOIR SOLUTION BY VAPOR DIFFUSION (SITTING DROPS) AT 277 K.
Resolution 2.85 Å R-free 0.273
2C0O Src family kinase Hck with bound inhibitor A-770041 Deposited 2005-09-06 Different construct Different mutation/modification 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 80–525（446 aa） Fragment：SH3-SH2-SH1, RESIDUES 80-525
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) L2G N-(4-{1-[4-(4-ACETYLPIPERAZIN-1-YL)-TRANS-CYCLOHEXYL]-4-AMINO-1H-PYRAZOLO[3,4-D]PYRIMIDIN-3-YL}-2-METHOXYPHENYL)-1-METHYL-1H-INDOLE-2-CARBOXAMIDE × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；HCK (10 MG/ML IN 150 MM NACL, 20 MM TRIS.HCL PH 8.0) WAS MIXED WITH A-770041 [100 MM STOCK SOLUTION IN DMSO) TO GIVE A FINAL A-770041 CONCENTRATION OF 1 MM. HCK/A-770041 WAS THEN MIXED WITH RESERVOIR SOLUTION (12% PEG 6000, 3% 1,5-DIAMINOPENTANE, 20% GLYCEROL, 200 MM CA(OAC)2, 100 MM TRIS.HCL PH 8.0) AND EQUILBRATED AGAINST THE RESERVOIR SOLUTION BY VAPOR DIFFUSION (SITTING DROPS) AT 277 K.
Resolution 2.85 Å R-free 0.273
2C0T Src family kinase Hck with bound inhibitor A-641359 Deposited 2005-09-07 Different construct Different mutation/modification 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 80–525（446 aa） Fragment：SH3-SH2-SH1, RESIDUES 80-525
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) L3G N-(4-{4-AMINO-1-[1-(TETRAHYDRO-2H-PYRAN-4-YL)PIPERIDIN-4-YL]-1H-PYRAZOLO[3,4-D]PYRIMIDIN-3-YL}-2-METHOXYPHENYL)-1-METHYL-1H-INDOLE-2-CARBOXAMIDE × 1 CA CALCIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；CRYSTALLIZATION CONDITIONS: HCK (10 MG/ML IN 150 MM NACL, 20 MM TRIS.HCL PH 8.0) WAS MIXED WITH A-641359 [100 MM STOCK SOLUTION OF THE MALEIC ACID SALT IN DMSO) TO GIVE A FINAL A-641359 CONCENTRATION OF 1 MM. HCK/A-641359 WAS THEN MIXED WITH RESERVOIR SOLUTION (12% PEG 6000, 3% 1, 5-DIAMINOPENTANE, 20% GLYCEROL, 200 MM CA(OAC)2, 100 MM TRIS.HCL PH 8.0) AND EQUILBRATED AGAINST THE RESERVOIR SOLUTION BY VAPOR DIFFUSION (SITTING DROPS) AT 277 K.
Resolution 2.15 Å R-free 0.253
2C0T Src family kinase Hck with bound inhibitor A-641359 Deposited 2005-09-07 Different construct Different mutation/modification 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 80–525（446 aa） Fragment：SH3-SH2-SH1, RESIDUES 80-525
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) L3G N-(4-{4-AMINO-1-[1-(TETRAHYDRO-2H-PYRAN-4-YL)PIPERIDIN-4-YL]-1H-PYRAZOLO[3,4-D]PYRIMIDIN-3-YL}-2-METHOXYPHENYL)-1-METHYL-1H-INDOLE-2-CARBOXAMIDE × 1 CA CALCIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；CRYSTALLIZATION CONDITIONS: HCK (10 MG/ML IN 150 MM NACL, 20 MM TRIS.HCL PH 8.0) WAS MIXED WITH A-641359 [100 MM STOCK SOLUTION OF THE MALEIC ACID SALT IN DMSO) TO GIVE A FINAL A-641359 CONCENTRATION OF 1 MM. HCK/A-641359 WAS THEN MIXED WITH RESERVOIR SOLUTION (12% PEG 6000, 3% 1, 5-DIAMINOPENTANE, 20% GLYCEROL, 200 MM CA(OAC)2, 100 MM TRIS.HCL PH 8.0) AND EQUILBRATED AGAINST THE RESERVOIR SOLUTION BY VAPOR DIFFUSION (SITTING DROPS) AT 277 K.
Resolution 2.15 Å R-free 0.253
2HCK SRC FAMILY KINASE HCK-QUERCETIN COMPLEX Deposited 1997-02-25 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 79–526（448 aa） Fragment：SH3-SH2-KINASE-REGULATORY TAIL
Chain B 79–526（448 aa） Fragment：SH3-SH2-KINASE-REGULATORY TAIL
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) CA CALCIUM ION × 2 QUE 3,5,7,3',4'-PENTAHYDROXYFLAVONE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；292 K；HANGING DROPS (1UL) OF 50MG/ML PROTEIN AND 10MM QUERCETIN WERE MIXED WITH EQUAL VOLUMES OF RESERVOIR BUFFER CONTAINING 150 MM CALCIUM ACETATE, 100MM CACODYLATE (PH 6.5), 7% PEG 8000 AND 16% V/V ETHYLENE GLYCOL. THE MIXED DROPS WERE THEN SEEDED AND STORED AT 19 DEGREES C., temperature 292K
Resolution 3.00 Å R-free 0.311
2HK5 Hck Kinase in Complex with Lck targetted Inhibitor PG-1009247 Deposited 2006-07-03 Different construct 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 247–514（268 aa） Fragment：Kinase Domian (Residues 246-513)
Not recorded 1BM 3-{[2-(1H-BENZIMIDAZOL-1-YL)-6-{[2-(DIETHYLAMINO)ETHYL]AMINO}PYRIMIDIN-4-YL]AMINO}-4-METHYLPHENOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；288 K；0.5-3.0M Ammonium Sulfate or Sodium Formate or 18 - 28% PEG 10K + 0.1M HEPES or Tris, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 288K
Resolution 2.00 Å R-free 0.250
2OI3 NMR Structure Analysis of the Hematopoetic Cell Kinase SH3 Domain complexed with an artificial high affinity ligand (PD1) Deposited 2007-01-10 Different construct Different oligomeric state Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 60–140（81 aa） Fragment：SH3 domain, residues 60-140
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.7；298 K；Ionic strength (raw mmCIF value) 20mM KPO4, 20mM NaCl；Pressure 1
NMR sample composition 1.3mM Hck-SH3 U-13C, U-15N: 1.3mM PD1, 20mM KPO4, 20mM NaCl, pH 6.7, 93% H2O, 7% D2O | 93% H2O/7% D2O
Resolution not provided
2OJ2 NMR Structure Analysis of the Hematopoetic Cell Kinase SH3 Domain complexed with an artificial high affinity ligand (PD1) Deposited 2007-01-12 Different construct Different oligomeric state Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 60–140（81 aa） Fragment：SH3
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.7；298 K；Ionic strength (raw mmCIF value) 20mM KPO4, 20mM NaCl；Pressure 1
NMR sample composition 1.3mM Hck-SH3 U-13C, U-15N: 1.3mM PD1, 20mM KPO4, 20mM NaCl, pH=6.7 | 93% H2O/7% D2O
Resolution not provided
3HCK NMR ensemble of the uncomplexed human HCK SH2 domain, 20 structures Deposited 1997-03-31 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 140–245（106 aa） Fragment：SH2, RESIDUES 119 - 224 OF HUMAN HCK
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.4；301 K
Resolution not provided
3NHN Crystal structure of the SRC-family kinase HCK SH3-SH2-linker regulatory region Deposited 2010-06-14 Different construct Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 72–256（185 aa） Fragment：UNP residues 72-256, Hck-SH3-SH2-Linker fragment
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；25% (v/v) polyethylene glycol 3,350, 0.15 M KSCN, 0.05 M NaCl, and 1:100 dilution of Hck-SH3-SH2-linker crystal seeds (grown in 25% v/v polyethylene glycol 3,350, 0.1 M Tris pH 8.5, 0.2 M NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 2.61 Å R-free 0.176
3RBB HIV-1 NEF protein in complex with engineered HCK SH3 domain Deposited 2011-03-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 79–138（60 aa）
Mutation：E90Y, A91S, I92P, H93F, H94S, E95W EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；0.1 M Hepes, 8% ethylene glycol, 22% PEG 8000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.35 Å R-free 0.245
3RBB HIV-1 NEF protein in complex with engineered HCK SH3 domain Deposited 2011-03-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 79–138（60 aa）
Mutation：E90Y, A91S, I92P, H93F, H94S, E95W EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；0.1 M Hepes, 8% ethylene glycol, 22% PEG 8000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.35 Å R-free 0.245
3REA HIV-1 Nef protein in complex with engineered Hck-SH3 domain Deposited 2011-04-04 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 79–138（60 aa）
Mutation：E90V, A91S, I92W, H93S, H94P, E95D No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；285 K；100 mM Tris buffer, 5% ethylne glycol, 10% PEG 8000, 0.2 M MgCl2, 15 mM MnCl2, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 285K
Resolution 2.00 Å R-free 0.205
3REA HIV-1 Nef protein in complex with engineered Hck-SH3 domain Deposited 2011-04-04 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 79–138（60 aa）
Mutation：E90V, A91S, I92W, H93S, H94P, E95D No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；285 K；100 mM Tris buffer, 5% ethylne glycol, 10% PEG 8000, 0.2 M MgCl2, 15 mM MnCl2, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 285K
Resolution 2.00 Å R-free 0.205
3REB HIV-1 Nef protein in complex with engineered Hck-SH3 domain Deposited 2011-04-04 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 79–138（60 aa）
Mutation：E90V, A91S, I92W, H93S, H94P, E95D No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；285 K；100 mM Hepes, 0.05 M sodium citrate, 15% isopropanol, 30% glycerol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 285K
Resolution 3.45 Å R-free 0.243
3REB HIV-1 Nef protein in complex with engineered Hck-SH3 domain Deposited 2011-04-04 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 79–138（60 aa）
Mutation：E90V, A91S, I92W, H93S, H94P, E95D No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；285 K；100 mM Hepes, 0.05 M sodium citrate, 15% isopropanol, 30% glycerol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 285K
Resolution 3.45 Å R-free 0.243
3VRY Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 4-Amino-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-7-yl-cyclopentane Deposited 2012-04-21 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP residues 81-526
Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF) B43 4-Amino-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-7-yl-cyclopentane × 1 CL CHLORIDE ION × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；21% PEG 6000, 180mM calcium acetate, 18% glycerol, 100mM Tris, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 2.48 Å R-free 0.281
3VRY Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 4-Amino-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-7-yl-cyclopentane Deposited 2012-04-21 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP residues 81-526
Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF) B43 4-Amino-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-7-yl-cyclopentane × 1 CL CHLORIDE ION × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；21% PEG 6000, 180mM calcium acetate, 18% glycerol, 100mM Tris, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 2.48 Å R-free 0.281
3VRZ Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 1-[4-(4-amino-7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-5-yl)phenyl]-3-benzylurea Deposited 2012-04-21 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP residues 81-526
Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF) CA CALCIUM ION × 1 CL CHLORIDE ION × 1 VRZ 1-[4-(4-amino-7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-5-yl)phenyl]-3-benzylurea × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；288 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 288K
Resolution 2.22 Å R-free 0.267
3VRZ Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 1-[4-(4-amino-7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-5-yl)phenyl]-3-benzylurea Deposited 2012-04-21 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP residues 81-526
Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF) CA CALCIUM ION × 1 CL CHLORIDE ION × 1 VRZ 1-[4-(4-amino-7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-5-yl)phenyl]-3-benzylurea × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；288 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 288K
Resolution 2.22 Å R-free 0.267
3VS0 Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor N-[4-(4-amino-7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-5-yl)phenyl]benzamide Deposited 2012-04-21 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP residues 81-526
Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF) CA CALCIUM ION × 1 CL CHLORIDE ION × 1 VS0 N-[4-(4-amino-7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-5-yl)phenyl]benzamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 2.93 Å R-free 0.295
3VS0 Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor N-[4-(4-amino-7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-5-yl)phenyl]benzamide Deposited 2012-04-21 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP residues 81-526
Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF) CA CALCIUM ION × 1 CL CHLORIDE ION × 1 VS0 N-[4-(4-amino-7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-5-yl)phenyl]benzamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 2.93 Å R-free 0.295
3VS1 Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 1-[4-(4-amino-7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-5-yl)phenyl]-3-phenylurea Deposited 2012-04-21 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP residues 81-526
Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF) CA CALCIUM ION × 1 CL CHLORIDE ION × 1 VSA 1-[4-(4-amino-7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-5-yl)phenyl]-3-phenylurea × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；288 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 288K
Resolution 2.46 Å R-free 0.281
3VS1 Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 1-[4-(4-amino-7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-5-yl)phenyl]-3-phenylurea Deposited 2012-04-21 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP residues 81-526
Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF) CA CALCIUM ION × 1 CL CHLORIDE ION × 1 VSA 1-[4-(4-amino-7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-5-yl)phenyl]-3-phenylurea × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；288 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 288K
Resolution 2.46 Å R-free 0.281
3VS2 Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 7-[cis-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine Deposited 2012-04-21 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP residues 81-526
Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF) VSB 7-[cis-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine × 1 CA CALCIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；288 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 288K
Resolution 2.61 Å R-free 0.279
3VS2 Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 7-[cis-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine Deposited 2012-04-21 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP residues 81-526
Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF) VSB 7-[cis-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine × 1 CA CALCIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；288 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 288K
Resolution 2.61 Å R-free 0.279
3VS3 Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 7-[trans-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine Deposited 2012-04-21 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP residues 81-526
Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF) VSE 7-[trans-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine × 1 CA CALCIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；288 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 288K
Resolution 2.17 Å R-free 0.279
3VS3 Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 7-[trans-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine Deposited 2012-04-21 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP residues 81-526
Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF) VSE 7-[trans-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine × 1 CA CALCIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；288 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 288K
Resolution 2.17 Å R-free 0.279
3VS4 Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 5-(4-phenoxyphenyl)-7-(tetrahydro-2H-pyran-4-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine Deposited 2012-04-21 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP residues 81-526
Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF) CA CALCIUM ION × 1 CL CHLORIDE ION × 1 VSF 5-(4-phenoxyphenyl)-7-(tetrahydro-2H-pyran-4-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 2.75 Å R-free 0.265
3VS4 Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 5-(4-phenoxyphenyl)-7-(tetrahydro-2H-pyran-4-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine Deposited 2012-04-21 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP residues 81-526
Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF) CA CALCIUM ION × 1 CL CHLORIDE ION × 1 VSF 5-(4-phenoxyphenyl)-7-(tetrahydro-2H-pyran-4-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 2.75 Å R-free 0.265
3VS5 Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 7-(1-methylpiperidin-4-yl)-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine Deposited 2012-04-21 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP residues 81-526
Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF) VSG 7-(1-methylpiperidin-4-yl)-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 2.85 Å R-free 0.309
3VS5 Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 7-(1-methylpiperidin-4-yl)-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine Deposited 2012-04-21 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP residues 81-526
Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF) VSG 7-(1-methylpiperidin-4-yl)-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 2.85 Å R-free 0.309
3VS6 Crystal structure of HCK complexed with a pyrazolo-pyrimidine inhibitor tert-butyl {4-[4-amino-1-(propan-2-yl)-1H-pyrazolo[3,4-d]pyrimidin-3-yl]-2-methoxyphenyl}carbamate Deposited 2012-04-21 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP residues 81-526
Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF) CA CALCIUM ION × 2 CL CHLORIDE ION × 1 VSH tert-butyl {4-[4-amino-1-(propan-2-yl)-1H-pyrazolo[3,4-d]pyrimidin-3-yl]-2-methoxyphenyl}carbamate × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；277 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 9, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 2.37 Å R-free 0.280
3VS6 Crystal structure of HCK complexed with a pyrazolo-pyrimidine inhibitor tert-butyl {4-[4-amino-1-(propan-2-yl)-1H-pyrazolo[3,4-d]pyrimidin-3-yl]-2-methoxyphenyl}carbamate Deposited 2012-04-21 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP residues 81-526
Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF) CA CALCIUM ION × 2 CL CHLORIDE ION × 1 VSH tert-butyl {4-[4-amino-1-(propan-2-yl)-1H-pyrazolo[3,4-d]pyrimidin-3-yl]-2-methoxyphenyl}carbamate × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；277 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 9, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 2.37 Å R-free 0.280
3VS7 Crystal structure of HCK complexed with a pyrazolo-pyrimidine inhibitor 1-cyclopentyl-3-(1H-pyrrolo[2,3-b]pyridin-5-yl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine Deposited 2012-04-21 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP residues 81-526
Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF) KS1 1-cyclopentyl-3-(1H-pyrrolo[2,3-b]pyridin-5-yl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine × 1 CA CALCIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 3.00 Å R-free 0.290
3VS7 Crystal structure of HCK complexed with a pyrazolo-pyrimidine inhibitor 1-cyclopentyl-3-(1H-pyrrolo[2,3-b]pyridin-5-yl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine Deposited 2012-04-21 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP residues 81-526
Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF) KS1 1-cyclopentyl-3-(1H-pyrrolo[2,3-b]pyridin-5-yl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine × 1 CA CALCIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 3.00 Å R-free 0.290
4LUD Crystal Structure of HCK in complex with the fluorescent compound SKF86002 Deposited 2013-07-25 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP residues 81-526
Mutation：Q502E/Q503E/Q504I Non-standard monomer：Yes (specific site not provided by mmCIF) CA CALCIUM ION × 2 SK8 6-(4-fluorophenyl)-5-(pyridin-4-yl)-2,3-dihydroimidazo[2,1-b][1,3]thiazole × 1 GOL GLYCEROL × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；288 K；0.1M Tris, 0.1M Calcium Acetate, 20% Glycerol, 24% PEG 6000, 2mM SKF86002, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 288K
Resolution 2.85 Å R-free 0.261
4LUD Crystal Structure of HCK in complex with the fluorescent compound SKF86002 Deposited 2013-07-25 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP residues 81-526
Mutation：Q502E/Q503E/Q504I Non-standard monomer：Yes (specific site not provided by mmCIF) CA CALCIUM ION × 1 SK8 6-(4-fluorophenyl)-5-(pyridin-4-yl)-2,3-dihydroimidazo[2,1-b][1,3]thiazole × 1 GOL GLYCEROL × 2 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；288 K；0.1M Tris, 0.1M Calcium Acetate, 20% Glycerol, 24% PEG 6000, 2mM SKF86002, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 288K
Resolution 2.85 Å R-free 0.261
4LUE Crystal Structure of HCK in complex with 7-[trans-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine (resulting from displacement of SKF86002) Deposited 2013-07-25 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP residues 81-526
Mutation：Q502E/Q503E/Q504I Non-standard monomer：Yes (specific site not provided by mmCIF) CA CALCIUM ION × 1 VSE 7-[trans-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine × 1 CL CHLORIDE ION × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；288 K；0.1M Tris, 0.1M Calcium Acetate, 20% Glycerol, 24% PEG 6000, 2mM SKF86002, soaked with 2mM inhibitor in DMSO., pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 288K
Resolution 3.04 Å R-free 0.256
4LUE Crystal Structure of HCK in complex with 7-[trans-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine (resulting from displacement of SKF86002) Deposited 2013-07-25 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP residues 81-526
Mutation：Q502E/Q503E/Q504I Non-standard monomer：Yes (specific site not provided by mmCIF) CA CALCIUM ION × 1 VSE 7-[trans-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine × 1 CL CHLORIDE ION × 1 GOL GLYCEROL × 2 IMD IMIDAZOLE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；288 K；0.1M Tris, 0.1M Calcium Acetate, 20% Glycerol, 24% PEG 6000, 2mM SKF86002, soaked with 2mM inhibitor in DMSO., pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 288K
Resolution 3.04 Å R-free 0.256
4ORZ HIV-1 Nef protein in complex with single domain antibody sdAb19 and an engineered Hck SH3 domain Deposited 2014-02-12 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 77–138（62 aa） Fragment：SH3 domain, UNP residues 77-138
Mutation：E90Y, A91S, I92P, H93F, H94S, E95W No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；About 0.1 micro L of protein solution at 10 mg/ml concentration was mixed with 0.1 micro L of reservoir solution from a 70 L reservoir in 96-well Hampton 3553 crystallization plates. Initial crystals of NefSF2 sdAb19 SH3B6 could be obtained in 0.2 M potassium formate and 20% polyethylene glycol (PEG) 3350. Crystal conditions were optimized to 0.2 M potassium formate, 17.5% polyethylene glycol (PEG) 3350 and 0.35 M ammonium chloride grown by hanging-drop vapor diffusion in Linbro crystallization plates. , pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.00 Å R-free 0.236
4U5W Crystal Structure of HIV-1 Nef-SF2 Core Domain in Complex with the Src Family Kinase Hck SH3-SH2 Tandem Regulatory Domains Deposited 2014-07-25 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 × 4 PDB declaration: tetrameric
Chain B 72–242（171 aa） Fragment：SH3-SH2 domain, UNP residues 72-242
Chain D 72–242（171 aa） Fragment：SH3-SH2 domain, UNP residues 72-242
Not recorded MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 3 IOD IODIDE ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277.15 K；0.09 M ADA, pH 6.5, 10.8% (v/v) 2-methyl-2,4-pentanediol, 100 mM NaI
Resolution 1.86 Å R-free 0.195
5H09 Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor (S)-ethyl2-(((1r,4S)-4-(4-amino-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclohexyl)amino)-4-methylpentanoate Deposited 2016-10-04 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP RESIDUES 81-526
Mutation：Q523E, Q524E, Q525I Non-standard monomer：Yes (specific site not provided by mmCIF) OOO ethyl (2~{S})-2-[[4-[4-azanyl-5-(4-phenoxyphenyl)pyrrolo[2,3-d]pyrimidin-7-yl]cyclohexyl]amino]-4-methyl-pentanoate × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.22-0.25 M ammonium formate, 12-22 % PEG 3350
Resolution 1.95 Å R-free 0.223
5H0B Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor (S)-2-(((1r,4S)-4-(4-amino-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclohexyl)amino)-4-methylpentanoic acid Deposited 2016-10-04 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP RESIDUES 81-526
Mutation：Q523E, Q524E, Q525I Non-standard monomer：Yes (specific site not provided by mmCIF) OOQ (2~{S})-2-[[4-[4-azanyl-5-(4-phenoxyphenyl)pyrrolo[2,3-d]pyrimidin-7-yl]cyclohexyl]azaniumyl]-4-methyl-pentanoate × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.22-0.25 M ammonium formate, 12-22 % PEG 3350
Resolution 1.65 Å R-free 0.205
5H0E Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor (S)-2-(((1r,4S)-4-(4-amino-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclohexyl)amino)-4-methylpentanamide Deposited 2016-10-04 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP RESIDUES 81-526
Mutation：Q523E, Q524E, Q525I Non-standard monomer：Yes (specific site not provided by mmCIF) OOS (2~{S})-2-[[4-[4-azanyl-5-(4-phenoxyphenyl)pyrrolo[2,3-d]pyrimidin-7-yl]cyclohexyl]amino]-4-methyl-pentanamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.22-0.25M ammonium formate, 12-22% PEG 3350
Resolution 2.10 Å R-free 0.226
5H0G Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor (S)-2-(((1r,4S)-4-(4-amino-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclohexyl)amino)-N,4-dimethylpentanamide Deposited 2016-10-04 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP RESIDUES 81-526
Mutation：Q523E, Q524E, Q525I Non-standard monomer：Yes (specific site not provided by mmCIF) OOU (2~{S})-2-[[4-[4-azanyl-5-(4-phenoxyphenyl)pyrrolo[2,3-d]pyrimidin-7-yl]cyclohexyl]amino]-~{N},4-dimethyl-pentanamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.22-0.25 M ammonium formate, 12-22 % PEG 3350
Resolution 1.80 Å R-free 0.224
5H0H Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor (S)-2-(((1r,4S)-4-(4-amino-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclohexyl)amino)-N,N,4-trimethylpentanamide Deposited 2016-10-04 Different construct Different mutation/modification 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 81–526（446 aa） Fragment：UNP RESIDUES 81-526
Mutation：Q523E, Q524E, Q525I Non-standard monomer：Yes (specific site not provided by mmCIF) OOV (2~{S})-2-[[4-[4-azanyl-5-(4-phenoxyphenyl)pyrrolo[2,3-d]pyrimidin-7-yl]cyclohexyl]amino]-~{N},~{N},4-trimethyl-pentanamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.22-0.25 M ammonium formate, 12-22 % PEG 3350
Resolution 1.72 Å R-free 0.224
5HCK HUMAN HCK SH3 DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1998-03-09 Parsed fields agree Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 72–143（72 aa） Fragment：SH3 DOMAIN
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.25；298 K
Resolution not provided
5NUH Crystal structure of SIVmac239 Nef bound to an engineered Hck SH3 domain Deposited 2017-04-30 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 78–90（13 aa）
Chain D 96–138（43 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；12% PEG 3350, 0.15 M tri-lithium-citrat, 1% 1.6 hexandiol
Resolution 2.78 Å R-free 0.229
5NUH Crystal structure of SIVmac239 Nef bound to an engineered Hck SH3 domain Deposited 2017-04-30 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 78–90（13 aa）
Chain C 96–138（43 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；12% PEG 3350, 0.15 M tri-lithium-citrat, 1% 1.6 hexandiol
Resolution 2.78 Å R-free 0.229
5ZJ6 Crystal structure of HCK kinase complexed with a pyrrolo-pyrimidine inhibitor 7-[trans-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine Deposited 2018-03-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 242–521（280 aa）
Chain B 242–521（280 aa）
Not recorded VSE 7-[trans-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；288 K；0.1 M Tris-HCl (pH 8.5) 25 % (v/v) PEG 10,000
Resolution 1.70 Å R-free 0.240
8F2P Nef SF2 dimerization mutant bound to Hck SH3 Deposited 2022-11-08 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 77–140（64 aa） Fragment：Hck SH3 domain (UNP residues 77-140)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；0.1 M sodium chloride, 0.1 M sodium acetate, pH 4.6, 12% v/v MPD
Resolution 2.63 Å R-free 0.252
9BYJ Crystal Structure of Hck in complex with the Src-family kinase inhibitor A-419259 Deposited 2024-05-23 Different construct Different mutation/modification 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 81–526（446 aa）
Mutation：Q523E,Q524E,Q525I Non-standard monomer：Yes (specific site not provided by mmCIF) VSE 7-[trans-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine × 1 EDO 1,2-ETHANEDIOL × 6 DMS DIMETHYL SULFOXIDE × 2 SCN THIOCYANATE ION × 15 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；10 mM Tris-HCl, pH 8.3, 75 mM NaCl, 5% glycerol, 2 mM TCEP, 0.1 M sodium thiocyanate, 10% w/v PEG 3350, 0.095 mM 7-[trans-4-(4-Methyl-1-piperazinyl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-Pyrrolo[2,3-d]pyrimidin-4-amine, 0.5 mM N~2~-{[2-(2,4-difluorophenoxy)pyridin-3-yl]methyl}-N~4~-isopropylpyrimidine-2,4-diamine,1 % DMSO
Resolution 1.80 Å R-free 0.219

39 other PDB entries and 59 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HCK_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–72； UniProt 72–143

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.

SAXS scattering curve SAXS Profile

SAXS profile for 4hck

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4hck
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4hck
Deposition date deposition_date1998-03-09
Structure title titleHUMAN HCK SH3 DOMAIN, NMR, 25 STRUCTURES
Keywords keywordsSH3, PROTEIN TYROSINE KINASE, SIGNAL TRANSDUCTION, TRANSFERASE; TRANSFERASE
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier11.11 Å
Radius of gyration Rg (electron density) rg_electron10.81 Å
Forward intensity I(0) i0435264000.00
Molecular weight molecular_weight175570.0 kDa
Excluded volume excluded_volume218520 ų
Envelope volume envelope_volume14121 ų
Hydration-shell volume shell_volume9889 ų
Envelope diameter envelope_diameter44.0 Å
Shell Rg shell_rg17.89 Å
Envelope Rg envelope_rg12.82 Å
Shape Rg shape_rg10.80 Å
Total Rg total_rg10.98 Å
Total atoms total_atoms24175
Residues n_residues1525
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax38.1 Å
Rg (real space) rg_real11.06 Å
Rg uncertainty (real space) rg_real_error0.29 Å
I(0) (real space) i0_real4.3530e+08
I(0) uncertainty (real space) i0_real_error4.7430e+06
Rg (reciprocal space) rg_reciprocal11.06 Å
I(0) (reciprocal space) i0_reciprocal435300000.0000
Solution quality estimate total_estimate0.8479
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.0 Å
Skewness Skewness skewness0.144
Kurtosis Kurtosis kurtosis-0.105
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha67880.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.686; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.962
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4hcka_
Class classb — All beta proteins
Fold Fold foldb.34 — SH3-like barrel
Superfamily Superfamily superfamilyb.34.2 — SH3-domain
Family Family familyb.34.2.1 — SH3-domain

CATH v4.4 (1 domains)

Domain ID domain_id4hckA00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily40 — SH3 Domains
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8. Citations (1)

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9. Files and Curves (10)