3SWS
Crystal Structure of the Quinone Form of Methylamine Dehydrogenase in Complex with the Diferric 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 400 |
| Chain | Residue |
| A | ASN66 |
| A | THR275 |
| A | PRO277 |
| A | HOH378 |
| A | HOH380 |
| A | HOH387 |
| A | HOH396 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 401 |
| Chain | Residue |
| A | HOH382 |
| A | HOH492 |
| A | HOH854 |
| A | HOH934 |
| A | ASN231 |
| A | THR233 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 402 |
| Chain | Residue |
| A | LEU250 |
| A | ARG252 |
| A | ILE255 |
| A | HOH777 |
| A | HOH947 |
| A | HOH1720 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEC A 500 |
| Chain | Residue |
| A | GLN29 |
| A | SER30 |
| 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 | GLN163 |
| A | LYS265 |
| A | HOH444 |
| A | HOH530 |
| A | HOH1570 |
| A | HOH2200 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEC A 600 |
| Chain | Residue |
| A | TRP93 |
| A | ASN200 |
| A | CYS201 |
| A | CYS204 |
| A | HIS205 |
| A | HIS224 |
| A | LEU228 |
| A | PHE264 |
| A | PRO267 |
| A | LEU269 |
| A | TYR278 |
| A | MET279 |
| A | HIS280 |
| A | LEU287 |
| A | TYR294 |
| A | HOH380 |
| A | HOH387 |
| A | HOH426 |
| A | HOH442 |
| A | HOH456 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 400 |
| Chain | Residue |
| B | ASN66 |
| B | THR275 |
| B | PRO277 |
| B | HOH383 |
| B | HOH399 |
| B | HOH417 |
| B | HOH443 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 401 |
| Chain | Residue |
| B | ASN231 |
| B | THR233 |
| B | HOH411 |
| B | HOH999 |
| B | HOH1109 |
| B | HOH1146 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 402 |
| Chain | Residue |
| B | LEU250 |
| B | ARG252 |
| B | ILE255 |
| B | HOH517 |
| B | HOH818 |
| B | HOH1261 |
| site_id | AC9 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE HEC B 500 |
| Chain | Residue |
| B | ALA104 |
| B | PRO107 |
| B | GLU113 |
| B | GLN163 |
| B | LYS265 |
| B | HOH407 |
| B | HOH549 |
| B | HOH605 |
| B | HOH770 |
| B | HOH901 |
| B | GLN29 |
| B | SER30 |
| B | CYS31 |
| B | CYS34 |
| B | HIS35 |
| B | SER54 |
| B | VAL55 |
| B | ARG65 |
| B | THR67 |
| B | PRO68 |
| B | LEU70 |
| B | GLN91 |
| B | PHE92 |
| B | TRP93 |
| B | ARG96 |
| B | LEU100 |
| B | GLN103 |
| site_id | BC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEC B 600 |
| Chain | Residue |
| B | ASN200 |
| B | CYS201 |
| B | CYS204 |
| B | HIS205 |
| B | HIS224 |
| B | LEU228 |
| B | PHE264 |
| B | PRO267 |
| B | LEU269 |
| B | TYR278 |
| B | MET279 |
| B | HIS280 |
| B | LEU287 |
| B | TYR294 |
| B | GLU327 |
| B | HOH375 |
| B | HOH399 |
| B | HOH417 |
| B | HOH423 |
| B | HOH430 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MES D 387 |
| Chain | Residue |
| A | GLU137 |
| A | ALA138 |
| A | LEU139 |
| A | GLY141 |
| D | ARG35 |
| D | LEU37 |
| D | GLU38 |
| D | HOH477 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO D 388 |
| Chain | Residue |
| C | HOH457 |
| D | GLY136 |
| D | THR137 |
| D | TRP282 |
| D | GLN378 |
| D | HOH695 |
| D | HOH1241 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 374 |
| Chain | Residue |
| B | GLU347 |
| B | LEU358 |
| B | HOH489 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 374 |
| Chain | Residue |
| A | ALA164 |
| A | ARG215 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT D 389 |
| Chain | Residue |
| D | ARG174 |
| D | LEU176 |
| D | ASP177 |
| D | THR211 |
| D | PRO212 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 1PE D 390 |
| Chain | Residue |
| D | THR187 |
| D | LYS236 |
| D | ALA237 |
| D | GLY238 |
| D | LEU254 |
| D | SER255 |
| D | HOH1365 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PG4 F 387 |
| Chain | Residue |
| F | THR187 |
| F | LYS236 |
| F | SER255 |
| F | GLY257 |
| F | HOH851 |
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 | TRQ57 | 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 | TRQ57 | 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 |
