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1OPL

Structural basis for the auto-inhibition of c-Abl tyrosine kinase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MYR A 538
ChainResidue
ALEU360
AGLU481
AILE521
ALEU529

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE P16 A 539
ChainResidue
AMET309
AILE332
ATHR334
AGLU335
AMET337
AGLY340
ALEU389
AALA399
AASP400
APHE401
ATYR272
AVAL275
AALA288
ALYS290
AGLU305

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE P16 B 538
ChainResidue
BTYR272
BGLU305
BMET309
BTHR334
BGLU335
BMET337
BGLY340
BLEU389
BALA399
BPHE401

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues180
DetailsDomain: {"description":"SH2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00191","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues502
DetailsDomain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues48
DetailsMotif: {"description":"Kinase activation loop"}
ChainResidueDetails

site_idSWS_FT_FI4
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_FI5
Number of Residues30
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"16912036","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18775435","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues11
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"16912036","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"16912036","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P42684","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues6
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases","evidences":[{"source":"PubMed","id":"16912036","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00520","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AARG386
AASN382

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BARG386
BASN382

239803

PDB entries from 2025-08-06

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