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1OPJ

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

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 Residues2
DetailsBINDING SITE FOR RESIDUE CL A 5
ChainResidue
ASTI3
AILE379

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 6
ChainResidue
BSTI4
BILE379

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MYR A 1
ChainResidue
ALEU360
AALA363
ALEU448

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MYR B 2
ChainResidue
BGLU481
BGLY482
BVAL525
BLEU529
BASN250
BLEU360

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE STI A 3
ChainResidue
ACL5
AHOH22
AVAL275
AALA288
ALYS290
AGLU305
AMET309
AVAL318
AILE332
ATHR334
APHE336
AMET337
AILE379
AHIS380
AALA399
AASP400
APHE401

site_idAC6
Number of Residues17
DetailsBINDING SITE FOR RESIDUE STI B 4
ChainResidue
BCL6
BHOH47
BTYR272
BVAL275
BALA288
BLYS290
BGLU305
BMET309
BILE332
BTHR334
BPHE336
BMET337
BILE379
BHIS380
BALA399
BASP400
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

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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP382
BASP382

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
ALEU267
AGLU335
BLEU267
BGLU335

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALYS290
BLYS290

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P42684
ChainResidueDetails
ASER248
BSER248

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P00519
ChainResidueDetails
ATYR272
ATYR276
ATYR432
BTYR272
BTYR276
BTYR432

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases => ECO:0000269|PubMed:10988075, ECO:0000269|PubMed:12748290
ChainResidueDetails
ATYR412
BTYR412

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:9109492
ChainResidueDetails
ASER465
BSER465

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AARG386
AASP382

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BARG386
BASP382

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AALA384
AASP382

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BALA384
BASP382

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AALA384
AASP382
AASN387

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BALA384
BASP382
BASN387

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PDB entries from 2024-07-24

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