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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
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29063833","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6AO5","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by PKB/AKT1","evidences":[{"source":"PubMed","id":"20086174","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"23972470","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"23972470","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29063833","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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