1MRO
METHYL-COENZYME M REDUCTASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0015948 | biological_process | methanogenesis |
| A | 0016740 | molecular_function | transferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050524 | molecular_function | coenzyme-B sulfoethylthiotransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0015948 | biological_process | methanogenesis |
| B | 0016740 | molecular_function | transferase activity |
| B | 0050524 | molecular_function | coenzyme-B sulfoethylthiotransferase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0015948 | biological_process | methanogenesis |
| C | 0016740 | molecular_function | transferase activity |
| C | 0050524 | molecular_function | coenzyme-B sulfoethylthiotransferase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0015948 | biological_process | methanogenesis |
| D | 0016740 | molecular_function | transferase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050524 | molecular_function | coenzyme-B sulfoethylthiotransferase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0015948 | biological_process | methanogenesis |
| E | 0016740 | molecular_function | transferase activity |
| E | 0050524 | molecular_function | coenzyme-B sulfoethylthiotransferase activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0015948 | biological_process | methanogenesis |
| F | 0016740 | molecular_function | transferase activity |
| F | 0050524 | molecular_function | coenzyme-B sulfoethylthiotransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ZN A 801 |
| Chain | Residue |
| A | ARG102 |
| A | SER215 |
| A | ARG216 |
| A | CYS218 |
| D | ARG102 |
| D | SER215 |
| D | ARG216 |
| D | CYS218 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA F 802 |
| Chain | Residue |
| F | GLU30 |
| F | HOH8034 |
| F | HOH8122 |
| F | HOH8217 |
| F | HOH8225 |
| F | HOH8267 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA C 803 |
| Chain | Residue |
| C | GLU30 |
| C | HOH8044 |
| C | HOH8195 |
| C | HOH8213 |
| C | HOH8338 |
| site_id | AC4 |
| Number of Residues | 40 |
| Details | BINDING SITE FOR RESIDUE F43 A 700 |
| Chain | Residue |
| A | ALA144 |
| A | VAL145 |
| A | VAL146 |
| A | GLN147 |
| A | GLN230 |
| A | MET233 |
| A | ALA243 |
| A | HOH7583 |
| A | HOH7660 |
| A | HOH7680 |
| A | HOH7758 |
| A | HOH7792 |
| A | HOH7795 |
| D | GLY326 |
| D | GLY327 |
| D | VAL328 |
| D | GLY329 |
| D | PHE330 |
| D | THR331 |
| D | GLN332 |
| D | TYR333 |
| D | PHE396 |
| D | GLY397 |
| D | GLY442 |
| D | PHE443 |
| D | HOH7593 |
| D | COM9700 |
| E | SER365 |
| E | ILE366 |
| E | TYR367 |
| F | LEU117 |
| F | SER118 |
| F | GLY119 |
| F | ARG120 |
| F | LYS153 |
| F | SER154 |
| F | VAL155 |
| F | HIS156 |
| F | HIS158 |
| F | HOH7686 |
| site_id | AC5 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE F43 D 800 |
| Chain | Residue |
| A | GLY326 |
| A | GLY327 |
| A | VAL328 |
| A | GLY329 |
| A | PHE330 |
| A | THR331 |
| A | GLN332 |
| A | TYR333 |
| A | PHE396 |
| A | GLY397 |
| A | GLY442 |
| A | PHE443 |
| A | HOH7574 |
| A | COM9800 |
| B | SER365 |
| B | ILE366 |
| B | TYR367 |
| C | LEU117 |
| C | SER118 |
| C | GLY119 |
| C | LYS153 |
| C | SER154 |
| C | VAL155 |
| C | HIS156 |
| C | HIS158 |
| C | HOH7624 |
| D | ALA144 |
| D | VAL145 |
| D | VAL146 |
| D | GLN147 |
| D | GLN230 |
| D | MET233 |
| D | ALA243 |
| D | HOH7585 |
| D | HOH7606 |
| D | HOH7636 |
| D | HOH7644 |
| D | HOH7664 |
| D | HOH7740 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE TP7 A 9000 |
| Chain | Residue |
| A | ARG270 |
| A | LEU320 |
| A | MET324 |
| A | SER325 |
| A | PHE330 |
| A | PHE443 |
| A | MET480 |
| A | ASN481 |
| A | VAL482 |
| A | HOH7548 |
| A | HOH7578 |
| A | HOH7633 |
| A | HOH7679 |
| B | TYR367 |
| B | GLY369 |
| B | HIS379 |
| B | ILE380 |
| B | HOH7580 |
| D | ARG225 |
| D | LYS256 |
| D | MHS257 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE TP7 A 9500 |
| Chain | Residue |
| A | ARG225 |
| A | LYS256 |
| A | MHS257 |
| A | HOH7552 |
| A | HOH7567 |
| A | HOH7618 |
| A | HOH7724 |
| D | ARG270 |
| D | LEU320 |
| D | MET324 |
| D | PHE330 |
| D | PHE443 |
| D | MET480 |
| D | ASN481 |
| D | VAL482 |
| E | TYR367 |
| E | GLY369 |
| E | HIS379 |
| E | ILE380 |
| E | HOH7555 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE COM D 9700 |
| Chain | Residue |
| A | F43700 |
| D | TYR333 |
| D | PHE443 |
| D | TYR444 |
| E | PHE361 |
| E | SER365 |
| E | TYR367 |
| F | LEU117 |
| F | ARG120 |
| F | HOH7782 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE COM A 9800 |
| Chain | Residue |
| A | TYR333 |
| A | PHE443 |
| A | TYR444 |
| B | PHE361 |
| B | SER365 |
| B | TYR367 |
| C | LEU117 |
| C | ARG120 |
| C | HOH7741 |
| D | F43800 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 804 |
| Chain | Residue |
| A | SER224 |
| A | LYS256 |
| A | HIS262 |
| A | GLU275 |
| A | HOH7956 |
| A | HOH7977 |
| D | HOH7916 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D 805 |
| Chain | Residue |
| D | ALA173 |
| D | ASP174 |
| D | ASP183 |
| D | ASN185 |
| D | HOH7891 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 806 |
| Chain | Residue |
| A | HOH7800 |
| D | SER224 |
| D | LYS256 |
| D | GLU275 |
| D | HOH7968 |
| D | HOH7970 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 807 |
| Chain | Residue |
| A | ASP174 |
| A | ASP183 |
| A | ASN185 |
| A | HOH8004 |
| site_id | F43 |
| Number of Residues | 1 |
| Details | ACTIVE SITE |
| Chain | Residue |
| A | F43700 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11491299, ECO:0000269|PubMed:20707311, ECO:0000269|PubMed:21438550, ECO:0000269|PubMed:27467699, ECO:0007744|PDB:1HBN, ECO:0007744|PDB:3M1V, ECO:0007744|PDB:3POT, ECO:0007744|PDB:5A0Y |
| Chain | Residue | Details |
| C | GLN121 | |
| F | GLN121 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11491299, ECO:0000269|PubMed:20707311, ECO:0000269|PubMed:21438550, ECO:0000269|PubMed:27140643, ECO:0000269|PubMed:27467699, ECO:0000269|PubMed:9367957, ECO:0007744|PDB:1HBN, ECO:0007744|PDB:1MRO, ECO:0007744|PDB:3M1V, ECO:0007744|PDB:3POT, ECO:0007744|PDB:5A0Y, ECO:0007744|PDB:5G0R |
| Chain | Residue | Details |
| B | GLY370 | |
| E | GLY370 | |
| D | TRP226 | |
| D | MHS257 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: in chain B => ECO:0000269|PubMed:11491299, ECO:0000269|PubMed:20707311, ECO:0000269|PubMed:21438550, ECO:0000269|PubMed:27140643, ECO:0000269|PubMed:27467699, ECO:0000269|PubMed:9367957, ECO:0007744|PDB:1HBN, ECO:0007744|PDB:1MRO, ECO:0007744|PDB:3M1V, ECO:0007744|PDB:3POT, ECO:0007744|PDB:5A0Y, ECO:0007744|PDB:5G0R |
| Chain | Residue | Details |
| A | AGM271 | |
| D | AGM271 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11491299, ECO:0000269|PubMed:20707311, ECO:0000269|PubMed:21438550, ECO:0000269|PubMed:27467699, ECO:0000269|PubMed:9367957, ECO:0007744|PDB:1HBN, ECO:0007744|PDB:1MRO, ECO:0007744|PDB:3M1V, ECO:0007744|PDB:3POT, ECO:0007744|PDB:5A0Y |
| Chain | Residue | Details |
| A | ALA334 | |
| A | GL3445 | |
| D | ALA334 | |
| D | GL3445 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Pros-methylhistidine => ECO:0000269|PubMed:10660523, ECO:0000269|PubMed:11491299, ECO:0000269|PubMed:20707311, ECO:0000269|PubMed:21438550, ECO:0000269|PubMed:27467699, ECO:0000269|PubMed:9367957 |
| Chain | Residue | Details |
| A | ALA258 | |
| D | ALA258 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: 5-methylarginine => ECO:0000269|PubMed:10660523, ECO:0000269|PubMed:11491299, ECO:0000269|PubMed:20707311, ECO:0000269|PubMed:21438550, ECO:0000269|PubMed:27467699, ECO:0000269|PubMed:9367957 |
| Chain | Residue | Details |
| A | ALA272 | |
| D | ALA272 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: 2-methylglutamine => ECO:0000269|PubMed:10660523, ECO:0000269|PubMed:11491299, ECO:0000269|PubMed:20707311, ECO:0000269|PubMed:21438550, ECO:0000269|PubMed:27467699, ECO:0000269|PubMed:9367957 |
| Chain | Residue | Details |
| A | ARG401 | |
| D | ARG401 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: 1-thioglycine => ECO:0000269|PubMed:10660523, ECO:0000269|PubMed:11491299, ECO:0000269|PubMed:20707311, ECO:0000269|PubMed:21438550, ECO:0000269|PubMed:27467699, ECO:0000269|PubMed:9367957 |
| Chain | Residue | Details |
| A | TYR446 | |
| D | TYR446 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: (Z)-2,3-didehydroaspartate => ECO:0000269|PubMed:27467699 |
| Chain | Residue | Details |
| A | GLN451 | |
| D | GLN451 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | MOD_RES: S-methylcysteine => ECO:0000269|PubMed:10660523, ECO:0000269|PubMed:11491299, ECO:0000269|PubMed:20707311, ECO:0000269|PubMed:21438550, ECO:0000269|PubMed:27467699, ECO:0000269|PubMed:9367957 |
| Chain | Residue | Details |
| A | GLY453 | |
| D | GLY453 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 11023796, 11491299 |
| Chain | Residue | Details |
| A | GLY465 | |
| A | ASP501 |
| site_id | MCSA1 |
| Number of Residues | 1 |
| Details | M-CSA 156 |
| Chain | Residue | Details |
| B | GLY368 | electrostatic stabiliser, proton acceptor, proton donor, proton relay, radical stabiliser |
| A | ALA334 | electrostatic stabiliser, radical stabiliser |
| A | TYR446 | single electron acceptor, single electron donor, single electron relay |
| A | VAL482 | activator, electrostatic stabiliser, proton acceptor, proton donor, proton relay |
| site_id | MCSA2 |
| Number of Residues | 1 |
| Details | M-CSA 156 |
| Chain | Residue | Details |
| E | GLY368 | electrostatic stabiliser, proton acceptor, proton donor, proton relay, radical stabiliser |
| D | ALA334 | electrostatic stabiliser, radical stabiliser |
| D | TYR446 | single electron acceptor, single electron donor, single electron relay |
| D | VAL482 | activator, electrostatic stabiliser, proton acceptor, proton donor, proton relay |
