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3K5V

Structure of Abl kinase in complex with imatinib and GNF-2

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 Residues16
DetailsBINDING SITE FOR RESIDUE STJ A 1
ChainResidue
AALA356
APRO484
APHE512
AILE521
ALEU529
AHOH536
AHOH561
AHOH619
ALEU359
ALEU360
AALA363
ALEU448
AILE451
AALA452
ATYR454
AGLU481

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE STI A 2
ChainResidue
AHOH22
AALA288
ALYS290
AGLU305
AMET309
AILE312
AVAL318
AILE332
ATHR334
APHE336
AMET337
AILE379
AHIS380
AALA399
AASP400
APHE401

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE STJ B 1
ChainResidue
BLEU359
BLEU360
BALA363
BLEU448
BILE451
BALA452
BGLU481
BVAL487
BPHE512
BHOH619

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE STI B 2
ChainResidue
BHOH47
BLEU267
BVAL275
BALA288
BLYS290
BGLU305
BMET309
BILE312
BVAL318
BILE332
BTHR334
BMET337
BILE379
BHIS380
BALA399
BASP400
BPHE401

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 5
ChainResidue
AILE379
AHOH660
AHOH679

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGGGQYGEVYeGvwkkyslt..........VAVK
ChainResidueDetails
ALEU267-LYS290

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FIHrDLAARNCLV
ChainResidueDetails
APHE378-VAL390

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues48
DetailsMotif: {"description":"Kinase activation loop"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues28
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P42684","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P00519","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases","evidences":[{"source":"PubMed","id":"10988075","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12748290","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"9109492","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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