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4BC6

Crystal structure of human serine threonine kinase-10 bound to novel Bosutinib Isoform 1, previously thought to be Bosutinib

Replaces:  3ZZ2
Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE XZN A 1317
ChainResidue
ALEU42
ACYS113
APRO114
AGLU124
ALEU164
AASP175
AHOH2035
AALA63
ALYS65
AGLU81
AVAL94
AILE108
AILE110
AGLU111
APHE112

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1318
ChainResidue
ATHR130
APRO132
AGLN133
AALA302
AGLU305
AHOH2044

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGDGAFGKVYkAknketgal..........AAAK
ChainResidueDetails
ALEU42-LYS65

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKagNVLM
ChainResidueDetails
AILE153-MET165

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:PRU10027
ChainResidueDetails
AASP157

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU42

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
ALYS65

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER191

220113

PDB entries from 2024-05-22

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