3SXT
Crystal Structure of the Quinol Form of Methylamine Dehydrogenase in Complex with the Diferrous Form of MauG
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004130 | molecular_function | cytochrome-c peroxidase activity |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0004130 | molecular_function | cytochrome-c peroxidase activity |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0020037 | molecular_function | heme binding |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0098869 | biological_process | cellular oxidant detoxification |
| C | 0009308 | biological_process | amine metabolic process |
| C | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
| C | 0030058 | molecular_function | aliphatic amine dehydrogenase activity |
| C | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0052876 | molecular_function | methylamine dehydrogenase (amicyanin) activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0030058 | molecular_function | aliphatic amine dehydrogenase activity |
| D | 0030416 | biological_process | methylamine metabolic process |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0052876 | molecular_function | methylamine dehydrogenase (amicyanin) activity |
| E | 0009308 | biological_process | amine metabolic process |
| E | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
| E | 0030058 | molecular_function | aliphatic amine dehydrogenase activity |
| E | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| E | 0042597 | cellular_component | periplasmic space |
| E | 0052876 | molecular_function | methylamine dehydrogenase (amicyanin) activity |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0030058 | molecular_function | aliphatic amine dehydrogenase activity |
| F | 0030416 | biological_process | methylamine metabolic process |
| F | 0042597 | cellular_component | periplasmic space |
| F | 0052876 | molecular_function | methylamine dehydrogenase (amicyanin) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 401 |
| Chain | Residue |
| A | ASN66 |
| A | THR275 |
| A | PRO277 |
| A | HOH505 |
| A | HOH506 |
| A | HOH513 |
| A | HOH522 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 402 |
| Chain | Residue |
| A | HOH508 |
| A | HOH593 |
| A | HOH650 |
| A | HOH665 |
| A | ASN231 |
| A | THR233 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 403 |
| Chain | Residue |
| A | LEU250 |
| A | ARG252 |
| A | ILE255 |
| A | HOH640 |
| A | HOH666 |
| A | HOH757 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEC A 404 |
| Chain | Residue |
| A | GLN29 |
| A | CYS31 |
| A | CYS34 |
| A | HIS35 |
| A | VAL55 |
| A | ARG65 |
| A | THR67 |
| A | PRO68 |
| A | LEU70 |
| A | GLN91 |
| A | PHE92 |
| A | TRP93 |
| A | ARG96 |
| A | LEU100 |
| A | GLN103 |
| A | ALA104 |
| A | PRO107 |
| A | MET114 |
| A | GLN163 |
| A | LYS265 |
| A | HOH567 |
| A | HOH601 |
| A | HOH747 |
| A | HOH834 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEC A 405 |
| Chain | Residue |
| A | TRP93 |
| A | ASN200 |
| A | CYS201 |
| A | CYS204 |
| A | HIS205 |
| A | HIS224 |
| A | LEU228 |
| A | PHE264 |
| A | PRO267 |
| A | TYR278 |
| A | MET279 |
| A | HIS280 |
| A | LEU287 |
| A | TYR294 |
| A | SER324 |
| A | GLU327 |
| A | HOH506 |
| A | HOH513 |
| A | HOH549 |
| A | HOH565 |
| A | HOH578 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 406 |
| Chain | Residue |
| A | ALA164 |
| A | ARG215 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 407 |
| Chain | Residue |
| A | GLU347 |
| A | LEU358 |
| A | HOH744 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 401 |
| Chain | Residue |
| B | ASN66 |
| B | THR275 |
| B | PRO277 |
| B | HOH511 |
| B | HOH526 |
| B | HOH539 |
| B | HOH566 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 402 |
| Chain | Residue |
| B | ASN231 |
| B | THR233 |
| B | HOH534 |
| B | HOH681 |
| B | HOH700 |
| B | HOH704 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 403 |
| Chain | Residue |
| B | LEU250 |
| B | ARG252 |
| B | ILE255 |
| B | HOH590 |
| B | HOH642 |
| B | HOH720 |
| site_id | BC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEC B 404 |
| Chain | Residue |
| B | PHE92 |
| B | TRP93 |
| B | ARG96 |
| B | LEU100 |
| B | GLN103 |
| B | ALA104 |
| B | PRO107 |
| B | MET114 |
| B | GLN163 |
| B | LYS265 |
| B | HOH597 |
| B | HOH606 |
| B | HOH659 |
| B | GLN29 |
| B | SER30 |
| B | CYS31 |
| B | CYS34 |
| B | HIS35 |
| B | VAL55 |
| B | ARG65 |
| B | THR67 |
| B | PRO68 |
| B | LEU70 |
| B | GLN91 |
| site_id | BC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEC B 405 |
| Chain | Residue |
| B | TRP93 |
| B | ASN200 |
| B | CYS201 |
| B | CYS204 |
| B | HIS205 |
| B | HIS224 |
| B | LEU228 |
| B | PHE264 |
| B | PRO267 |
| B | TYR278 |
| B | MET279 |
| B | HIS280 |
| B | LEU287 |
| B | TYR294 |
| B | HOH501 |
| B | HOH526 |
| B | HOH539 |
| B | HOH545 |
| B | HOH552 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 406 |
| Chain | Residue |
| B | VAL230 |
| B | GLU318 |
| B | HOH537 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO D 401 |
| Chain | Residue |
| D | GLU38 |
| D | ARG70 |
| D | ILE72 |
| D | HOH555 |
| D | HOH722 |
| D | HOH873 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO F 401 |
| Chain | Residue |
| D | GLU328 |
| F | ASP124 |
| F | GLU126 |
| F | LYS170 |
| F | HOH597 |
| F | HOH695 |
| F | HOH702 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Tryptophylquinone","evidences":[{"source":"PubMed","id":"1409575","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 13 |
| Chain | Residue | Details |
| C | ASP32 | electrostatic stabiliser, proton acceptor, proton donor |
| C | TOQ57 | proton acceptor, proton donor, proton relay |
| C | TYR80 | electrostatic stabiliser, proton acceptor, proton donor |
| C | ALA112 | proton acceptor, proton donor, proton relay, single electron donor |
| C | ILE123 | steric role |
| C | ILE126 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 13 |
| Chain | Residue | Details |
| E | ASP32 | electrostatic stabiliser, proton acceptor, proton donor |
| E | TOQ57 | proton acceptor, proton donor, proton relay |
| E | TYR80 | electrostatic stabiliser, proton acceptor, proton donor |
| E | ALA112 | proton acceptor, proton donor, proton relay, single electron donor |
| E | ILE123 | steric role |
| E | ILE126 | electrostatic stabiliser |
