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5DH3

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 PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue 5BS A 401
ChainResidue
ALEU33
AGLU100
ATYR101
ACYS102
AGLY103
AGLY105
AASP109
ALEU153
AASP164

site_idAC2
Number of Residues1
Detailsbinding site for residue CL A 402
ChainResidue
ALYS132

site_idAC3
Number of Residues11
Detailsbinding site for residue 5BS B 401
ChainResidue
BLEU33
BVAL41
BALA54
BGLU100
BTYR101
BCYS102
BASP109
BLEU153
BALA163
BLYS298
BHOH525

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 B 402
ChainResidue
BCYS102
BGLY103
BASN155
BTHR156

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGSYGSVFkAihkesgqv..........VAIK
ChainResidueDetails
ALEU33-LYS56

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AASP146
BASP146

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU33
BLEU33

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ALYS56
BLYS56

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:29063833, ECO:0007744|PDB:6AO5
ChainResidueDetails
AASN151
AASP164
BASN151
BASP164

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PLK1 => ECO:0000269|PubMed:21723128, ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER15
BSER15

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PKB/AKT1 => ECO:0000269|PubMed:20086174, ECO:0000269|PubMed:20231902
ChainResidueDetails
ATHR117
BTHR117

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:23972470
ChainResidueDetails
ATPO174
BTPO174

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:23972470, ECO:0000269|PubMed:29063833
ChainResidueDetails
ATPO180
BTPO180

225158

PDB entries from 2024-09-18

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