5WQJ
Crystal structure of 3-Mercaptopyruvate Sulfurtransferase(3MST) in complex with compound1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001822 | biological_process | kidney development |
A | 0001889 | biological_process | liver development |
A | 0004792 | molecular_function | thiosulfate sulfurtransferase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005743 | cellular_component | mitochondrial inner membrane |
A | 0016740 | molecular_function | transferase activity |
A | 0016783 | molecular_function | sulfurtransferase activity |
A | 0016784 | molecular_function | 3-mercaptopyruvate sulfurtransferase activity |
A | 0019346 | biological_process | transsulfuration |
A | 0021510 | biological_process | spinal cord development |
A | 0042802 | molecular_function | identical protein binding |
A | 0043005 | cellular_component | neuron projection |
A | 0045202 | cellular_component | synapse |
A | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
B | 0001822 | biological_process | kidney development |
B | 0001889 | biological_process | liver development |
B | 0004792 | molecular_function | thiosulfate sulfurtransferase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005743 | cellular_component | mitochondrial inner membrane |
B | 0016740 | molecular_function | transferase activity |
B | 0016783 | molecular_function | sulfurtransferase activity |
B | 0016784 | molecular_function | 3-mercaptopyruvate sulfurtransferase activity |
B | 0019346 | biological_process | transsulfuration |
B | 0021510 | biological_process | spinal cord development |
B | 0042802 | molecular_function | identical protein binding |
B | 0043005 | cellular_component | neuron projection |
B | 0045202 | cellular_component | synapse |
B | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | binding site for residue 7N3 A 301 |
Chain | Residue |
A | TRP36 |
A | GLY249 |
A | SER250 |
A | VAL252 |
A | THR253 |
A | HOH413 |
A | HOH420 |
A | HOH458 |
A | HOH528 |
A | PRO39 |
A | ASP73 |
A | HIS74 |
A | TYR108 |
A | ARG188 |
A | PRO196 |
A | ARG197 |
A | CSS248 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue NA A 302 |
Chain | Residue |
A | ASP73 |
A | HIS74 |
A | MET75 |
A | SER250 |
A | ASP273 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue NA A 303 |
Chain | Residue |
A | GLU195 |
A | ARG197 |
A | ILE200 |
A | HOH517 |
A | HOH572 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue NA A 304 |
Chain | Residue |
A | ARG46 |
A | SER147 |
site_id | AC5 |
Number of Residues | 16 |
Details | binding site for residue 7N3 B 301 |
Chain | Residue |
B | TRP36 |
B | PRO39 |
B | ASP73 |
B | HIS74 |
B | TYR108 |
B | ARG188 |
B | PRO196 |
B | ARG197 |
B | CSS248 |
B | GLY249 |
B | SER250 |
B | VAL252 |
B | HOH435 |
B | HOH441 |
B | HOH467 |
B | HOH512 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue NA B 302 |
Chain | Residue |
B | ASP73 |
B | HIS74 |
B | MET75 |
B | SER250 |
B | ASP273 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue NA B 303 |
Chain | Residue |
B | GLU195 |
B | ARG197 |
B | ILE200 |
B | HOH559 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Cysteine persulfide intermediate => ECO:0000255|PROSITE-ProRule:PRU00173, ECO:0000269|PubMed:18855522, ECO:0000269|PubMed:28079151 |
Chain | Residue | Details |
A | CSS248 | |
B | CSS248 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ARG188 | |
B | ARG188 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P25325 |
Chain | Residue | Details |
A | ALA2 | |
B | ALA2 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P25325 |
Chain | Residue | Details |
A | SER35 | |
B | SER35 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337 |
Chain | Residue | Details |
A | LYS40 | |
B | LYS40 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine => ECO:0007744|PubMed:23806337 |
Chain | Residue | Details |
A | LYS146 | |
A | LYS164 | |
B | LYS146 | |
B | LYS164 |