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6AO5

Crystal structure of human MST2 in complex with SAV1 SARAH domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
A0007165biological_processsignal transduction
B0006915biological_processapoptotic process
B0007165biological_processsignal transduction
B0035329biological_processhippo signaling
B0042127biological_processregulation of cell population proliferation
B0060090molecular_functionmolecular adaptor activity
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue ANP A 501
ChainResidue
AGLU35
AASP109
AASN146
ALYS148
AGLY150
AASN151
ALEU153
AASP164
AMG502
ASER37
ATYR38
AVAL41
ALYS56
AMET99
AGLU100
ACYS102
ASER106

site_idAC2
Number of Residues4
Detailsbinding site for residue MG A 502
ChainResidue
AGLY150
AASN151
AASP164
AANP501

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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AASN146

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU33

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING:
ChainResidueDetails
ALYS56

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:29063833, ECO:0007744|PDB:6AO5
ChainResidueDetails
AASN151
AASP164

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Cleavage; by caspase-3
ChainResidueDetails
AASP436

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PKB/AKT1 => ECO:0000269|PubMed:20086174, ECO:0000269|PubMed:20231902
ChainResidueDetails
ATHR117

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:23972470
ChainResidueDetails
ATHR174

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:23972470, ECO:0000269|PubMed:29063833
ChainResidueDetails
ATHR180

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ALYS430

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:29063833
ChainResidueDetails
AMET450

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:29063833, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PKB/AKT1 => ECO:0000269|PubMed:20086174
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER444

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PDB entries from 2024-07-10

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