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2FO0

Organization of the SH3-SH2 Unit in Active and Inactive Forms of the c-Abl Tyrosine Kinase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MYR A 701
ChainResidue
AGLU481
AILE521

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE P16 A 702
ChainResidue
AGLU335
APHE336
AMET337
AGLY340
ALEU389
AALA399
AASP400
ATYR272
AVAL275
AALA288
ALYS290
AGLU305
AMET309
ATHR334

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 703
ChainResidue
ATYR345
AGLY391
AGLU392
AASN393
AHIS394

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 704
ChainResidue
ATHR197
AALA198
ATHR296
AMET297

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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASN382

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING:
ChainResidueDetails
ALYS290
AGLU335
ALEU267

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:16543148, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332
ChainResidueDetails
ASEP69

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16912036, ECO:0000269|PubMed:18775435
ChainResidueDetails
ATYR89

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:16912036
ChainResidueDetails
ATYR147
ATYR158
ATYR191
ATYR204
ATYR234
ATYR134

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16912036
ChainResidueDetails
ATYR245

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P42684
ChainResidueDetails
ASER248

site_idSWS_FT_FI8
Number of Residues3
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATYR276
ATYR432
ATYR272

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases => ECO:0000269|PubMed:16912036
ChainResidueDetails
ATYR412

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00520
ChainResidueDetails
ASER465

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PDB entries from 2024-04-17

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