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3QRI

The crystal structure of human abl1 kinase domain in complex with DCC-2036

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 Residues19
DetailsBINDING SITE FOR RESIDUE 919 A 500
ChainResidue
AHOH41
AILE313
ATHR315
AGLU316
APHE317
AMET318
APHE359
AHIS361
AALA380
AASP381
APHE382
AHOH53
ALEU248
AVAL256
AALA269
ALYS271
AGLU286
AMET290
AVAL299

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 919 B 2
ChainResidue
BLEU248
BVAL256
BALA269
BLYS271
BGLU286
BMET290
BVAL299
BTHR315
BGLU316
BMET318
BLEU370
BALA380
BASP381
BPHE382
BHOH570

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 Residues6
DetailsBINDING:
ChainResidueDetails
ALEU248
ALYS271
AGLU316
BLEU248
BLYS271
BGLU316

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P42684
ChainResidueDetails
ASER229
BSER229

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATYR253
ATYR257
ATYR413
BTYR253
BTYR257
BTYR413

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases => ECO:0000269|PubMed:16912036
ChainResidueDetails
ATYR393
BTYR393

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00520
ChainResidueDetails
ASER446
BSER446

222415

PDB entries from 2024-07-10

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