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4QMS

MST3 in complex with DASATINIB

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 Residues11
DetailsBINDING SITE FOR RESIDUE 1N1 A 401
ChainResidue
AILE30
AHOH568
AHOH647
AALA51
ALYS53
AGLU70
AMET99
AGLU100
ATYR101
ALEU102
AGLY103

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 402
ChainResidue
ATHR238
ALYS248
AGLU249
AGLU252
AHOH509
AHOH601

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 403
ChainResidue
AGLY103
ASER153
AGLU154

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGSFGEVFkGidnrtqkv..........VAIK
ChainResidueDetails
AILE30-LYS53

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AGLY156

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING:
ChainResidueDetails
AILE42
AGLU65
AGLU112
AALA161
AILE174

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PKA => ECO:0000269|PubMed:10644707
ChainResidueDetails
AALA18

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:17046825, ECO:0000269|PubMed:19604147, ECO:0000269|PubMed:20124694, ECO:0007744|PubMed:23186163
ChainResidueDetails
AVAL190

227111

PDB entries from 2024-11-06

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