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8A66

Crystal structure of MST2 in complex with XMU-MP-1

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 PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGSYGSVFkAihkesgqv..........VAIK
ChainResidueDetails
ALEU135-LYS158
BLEU135-LYS158

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BASP248

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BLEU135

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING:
ChainResidueDetails
BLYS158

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:29063833, ECO:0007744|PDB:6AO5
ChainResidueDetails
BASN253
BASP266

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PKB/AKT1 => ECO:0000269|PubMed:20086174, ECO:0000269|PubMed:20231902
ChainResidueDetails
BTHR219

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:23972470
ChainResidueDetails
BTPO276

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:23972470, ECO:0000269|PubMed:29063833
ChainResidueDetails
BTPO283

224201

PDB entries from 2024-08-28

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