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3OEZ

crystal structure of the L317I mutant of the chicken c-Src tyrosine kinase domain complexed with imatinib

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 Residues18
DetailsBINDING SITE FOR RESIDUE STI A 601
ChainResidue
AHOH236
ATHR338
ATYR340
AMET341
AVAL383
AHIS384
AARG385
AALA403
AASP404
APHE405
AVAL281
AALA293
AILE294
ALYS295
AGLU310
AMET314
AVAL323
AILE336

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 1
ChainResidue
AASN397
AARG438

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 534
ChainResidue
AHOH192
AGLU517
AASP518
AHOH553
BLYS427
BVAL461
BPRO464
BGLY465

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE STI B 601
ChainResidue
BVAL281
BALA293
BLYS295
BGLU310
BVAL313
BMET314
BILE336
BTHR338
BTYR340
BMET341
BVAL383
BHIS384
BARG385
BLEU393
BALA403
BASP404
BPHE405

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

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP386
BASP386

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU273
BLEU273

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ALYS295
BLYS295

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:6273838, ECO:0000269|PubMed:8856081
ChainResidueDetails
ATYR416
BTYR416

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:8856081
ChainResidueDetails
ATYR436
BTYR436

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:19948721
ChainResidueDetails
ACYS498
BCYS498

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by CSK => ECO:0000269|PubMed:2420005
ChainResidueDetails
ATYR527
BTYR527

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PDB entries from 2024-10-09

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