7B2H
Crystal structure of the methyl-coenzyme M reductase from Methanothermobacter Marburgensis derivatized with xenon
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 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 | ARG120 | |
| F | ARG120 |
| 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 | GLY369 | |
| E | GLY369 | |
| D | ARG225 | |
| D | LYS256 |
| 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 | ARG270 | |
| D | ARG270 |
| 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 | TYR333 | |
| A | TYR444 | |
| D | TYR333 | |
| D | TYR444 |
| 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 | MHS257 | |
| D | MHS257 |
| 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 | AGM271 | |
| D | AGM271 |
| 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 | MGN400 | |
| D | MGN400 |
| 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 | GL3445 | |
| D | GL3445 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: (Z)-2,3-didehydroaspartate => ECO:0000269|PubMed:27467699 |
| Chain | Residue | Details |
| A | DYA450 | |
| D | DYA450 |
| 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 | SMC452 | |
| D | SMC452 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 1 |
| Details | M-CSA 156 |
| Chain | Residue | Details |
| B | TYR367 | electrostatic stabiliser, proton acceptor, proton donor, proton relay, radical stabiliser |
| A | TYR333 | electrostatic stabiliser, radical stabiliser |
| A | GL3445 | single electron acceptor, single electron donor, single electron relay |
| A | ASN481 | activator, electrostatic stabiliser, proton acceptor, proton donor, proton relay |
| site_id | MCSA2 |
| Number of Residues | 1 |
| Details | M-CSA 156 |
| Chain | Residue | Details |
| E | TYR367 | electrostatic stabiliser, proton acceptor, proton donor, proton relay, radical stabiliser |
| D | TYR333 | electrostatic stabiliser, radical stabiliser |
| D | GL3445 | single electron acceptor, single electron donor, single electron relay |
| D | ASN481 | activator, electrostatic stabiliser, proton acceptor, proton donor, proton relay |
