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1M52

Crystal Structure of the c-Abl Kinase domain in complex with PD173955

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 Residues7
DetailsBINDING SITE FOR RESIDUE MES B 117
ChainResidue
AARG367
APRO402
AILE403
ALYS404
ATRP405
ALEU445
BGLU466

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MES B 118
ChainResidue
BLYS404
BTRP405
BLEU445
BPRO402
BILE403

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE P17 A 119
ChainResidue
AGLY249
ATYR253
AVAL256
AALA269
ALYS271
AGLU286
AMET290
AILE313
ATHR315
AGLU316
AMET318
AGLY321
AALA380
AASP381
APHE382

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE P17 B 120
ChainResidue
BTYR253
BVAL256
BALA269
BLYS271
BGLU286
BMET290
BILE313
BTHR315
BGLU316
BMET318
BTHR319
BGLY321
BLEU370
BALA380
BASP381
BPHE382

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGGGQYGEVYeGvwkkyslt..........VAVK
ChainResidueDetails
ALEU248-LYS271

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FIHrDLAARNCLV
ChainResidueDetails
APHE359-VAL371

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
AASP363
BASP363

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
ALEU248
AGLU316
BLEU248
BGLU316

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALYS271
BLYS271

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P42684
ChainResidueDetails
ASER229
BSER229

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P00519
ChainResidueDetails
ATYR253
ATYR257
ATYR413
BTYR253
BTYR257
BTYR413

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
ATYR393
BTYR393

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:9109492
ChainResidueDetails
ASER446
BSER446

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP363
AARG367

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP363
BARG367

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP363
AALA365

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP363
BALA365

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN368
AASP363
AALA365

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASN368
BASP363
BALA365

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PDB entries from 2024-07-24

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