6AO5
Crystal structure of human MST2 in complex with SAV1 SARAH domain
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004674 | molecular_function | protein serine/threonine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
A | 0007165 | biological_process | signal transduction |
B | 0006915 | biological_process | apoptotic process |
B | 0007165 | biological_process | signal transduction |
B | 0035329 | biological_process | hippo signaling |
B | 0042127 | biological_process | regulation of cell population proliferation |
B | 0060090 | molecular_function | molecular adaptor activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | binding site for residue ANP A 501 |
Chain | Residue |
A | GLU35 |
A | ASP109 |
A | ASN146 |
A | LYS148 |
A | GLY150 |
A | ASN151 |
A | LEU153 |
A | ASP164 |
A | MG502 |
A | SER37 |
A | TYR38 |
A | VAL41 |
A | LYS56 |
A | MET99 |
A | GLU100 |
A | CYS102 |
A | SER106 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue MG A 502 |
Chain | Residue |
A | GLY150 |
A | ASN151 |
A | ASP164 |
A | ANP501 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGSYGSVFkAihkesgqv..........VAIK |
Chain | Residue | Details |
A | LEU33-LYS56 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | ASN146 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | LEU33 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS56 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:29063833, ECO:0007744|PDB:6AO5 |
Chain | Residue | Details |
A | ASN151 | |
A | ASP164 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | SITE: Cleavage; by caspase-3 |
Chain | Residue | Details |
A | ASP436 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by PKB/AKT1 => ECO:0000269|PubMed:20086174, ECO:0000269|PubMed:20231902 |
Chain | Residue | Details |
A | THR117 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:23972470 |
Chain | Residue | Details |
A | THR174 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:23972470, ECO:0000269|PubMed:29063833 |
Chain | Residue | Details |
A | THR180 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_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 |
Chain | Residue | Details |
A | LYS430 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:29063833 |
Chain | Residue | Details |
A | MET450 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:29063833, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by PKB/AKT1 => ECO:0000269|PubMed:20086174 |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195 |
Chain | Residue | Details |
A | SER444 |