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4QO9

MST3 IN COMPLEX WITH Danusertib

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PGE A 401
ChainResidue
AGLY87
ASER88
BGLN193

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 402
ChainResidue
APRO218
APRO237
ATHR238

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 403
ChainResidue
A627404

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 627 A 404
ChainResidue
ALYS53
AGLU100
ATYR101
ALEU102
AGLY103
AGLY104
AALA148
AASN149
ALEU151
ATYR291
ACL403
AHOH526
AHOH528
AHOH559
AILE30
AALA51

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DMS B 401
ChainResidue
BASP133
BSER137
BLYS266

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGE B 402
ChainResidue
AGLY241
BGLU28
BLYS40
BVAL49
BGLU154

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 403
ChainResidue
BGLU267
BHOH531
BHOH594

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 627 B 404
ChainResidue
BPHE35
BALA51
BLYS53
BMET99
BGLU100
BTYR101
BLEU102
BGLY103
BALA148
BALA161
BTYR291

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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AGLY156
BGLY156

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING:
ChainResidueDetails
AILE42
BILE174
AGLU65
AGLU112
AALA161
AILE174
BILE42
BGLU65
BGLU112
BALA161

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PKA => ECO:0000269|PubMed:10644707
ChainResidueDetails
AALA18
BALA18

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:17046825, ECO:0000269|PubMed:19604147, ECO:0000269|PubMed:20124694, ECO:0007744|PubMed:23186163
ChainResidueDetails
AVAL190
BVAL190

220113

PDB entries from 2024-05-22

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