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2G2I

A Src-like Inactive Conformation in the Abl Tyrosine Kinase Domain

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 ADP A 820
ChainResidue
AGLY249
AGLY250
AALA269
ATHR315
AGLU316
AMET318
ALEU370

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ADP B 821
ChainResidue
BVAL256
BALA269
BTHR315
BGLU316
BPHE317
BMET318
BGLY321
BASN322
BLEU370
BGLY249
BGLY250

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

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 2024-08-21

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