Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4QML

MST3 in complex with AMP-PNP

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 Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 401
ChainResidue
ATYR101
ALEU102
AGLY103
ASER153
AGLU154
AHOH541

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
AHOH653
AHOH654
AASP162
AANP403
AHOH651

site_idAC3
Number of Residues30
DetailsBINDING SITE FOR RESIDUE ANP A 403
ChainResidue
AGLY31
AGLY33
ASER34
AVAL38
AALA51
ALYS53
AMET99
AGLU100
ALEU102
ALEU151
AASP162
AMG402
AHOH561
AHOH563
AHOH565
AHOH567
AHOH569
AHOH572
AHOH579
AHOH583
AHOH585
AHOH611
AHOH629
AHOH632
AHOH636
AHOH638
AHOH651
AHOH652
AHOH653
AHOH654

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

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon