Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE B43 A 601
ChainResidue
ALEU273
AASP404
APHE405
AHOH701
AVAL281
AALA293
ALYS295
AVAL323
ATHR338
AGLU339
AMET341
ALEU393

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 602
ChainResidue
AARG85
AARG123
AARG128

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 603
ChainResidue
AGLU490
AHOH702
BGLU524
BPTR527

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA B 601
ChainResidue
AGLU524
APTR527
BGLU490

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE B43 B 602
ChainResidue
BLEU273
BVAL281
BALA293
BLYS295
BVAL323
BTHR338
BGLU339
BMET341
BLEU393
BASP404
BPHE405
BHOH711

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 603
ChainResidue
BARG123
BARG128

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues23
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGAGQFGEVWmAtynkhtk...........VAVK
ChainResidueDetails
ALEU273-LYS295

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YIHrDLRAANILV
ChainResidueDetails
ATYR382-VAL394

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
BASP386
AASP386

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
BLEU273
BLYS295
ALEU273
ALYS295

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ATHR207
BTHR207

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P08103
ChainResidueDetails
ATYR214
BTYR214

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:10644735, ECO:0000269|PubMed:11896602
ChainResidueDetails
BTYR416
ATYR416

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER467
BSER467

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:10360180, ECO:0000269|PubMed:10644735, ECO:0000269|PubMed:11896602, ECO:0000269|PubMed:16216497, ECO:0000269|PubMed:9024658
ChainResidueDetails
APTR527
BPTR527

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon