4O1Q
Crystal Structure of the Q103N-MauG/pre-Methylamine Dehydrogenase Complex
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 | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 401 |
| Chain | Residue |
| A | ASN66 |
| A | THR275 |
| A | PRO277 |
| A | HOH534 |
| A | HOH550 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE HEC A 402 |
| Chain | Residue |
| A | HIS35 |
| A | VAL55 |
| A | ARG65 |
| A | ASN66 |
| A | THR67 |
| A | PRO68 |
| A | LEU70 |
| A | GLN91 |
| A | PHE92 |
| A | TRP93 |
| A | ARG96 |
| A | LEU100 |
| A | ASN103 |
| A | ALA104 |
| A | PRO107 |
| A | GLU113 |
| A | MET114 |
| A | LEU159 |
| A | GLN163 |
| A | LYS265 |
| A | HOH535 |
| A | HOH563 |
| A | GLN29 |
| A | SER30 |
| A | CYS31 |
| A | CYS34 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEC A 403 |
| Chain | Residue |
| A | TRP93 |
| A | ASN200 |
| A | CYS201 |
| A | CYS204 |
| A | HIS205 |
| A | HIS224 |
| A | LEU228 |
| A | PHE264 |
| A | LYS265 |
| A | PRO267 |
| A | LEU269 |
| A | VAL272 |
| A | TYR278 |
| A | MET279 |
| A | HIS280 |
| A | LEU287 |
| A | TYR294 |
| A | GLU327 |
| A | LEU334 |
| A | HOH550 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 404 |
| Chain | Residue |
| A | LYS48 |
| A | GLN60 |
| A | ALA237 |
| A | HOH507 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 405 |
| Chain | Residue |
| A | LYS296 |
| A | SER299 |
| A | ARG300 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 401 |
| Chain | Residue |
| B | ASN66 |
| B | THR275 |
| B | PRO277 |
| B | HOH542 |
| B | HOH548 |
| B | HOH551 |
| B | HOH584 |
| site_id | AC7 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HEC B 402 |
| Chain | Residue |
| B | GLN29 |
| B | SER30 |
| B | CYS31 |
| B | CYS34 |
| B | HIS35 |
| B | ARG65 |
| B | ASN66 |
| B | THR67 |
| B | PRO68 |
| B | LEU70 |
| B | GLN91 |
| B | PHE92 |
| B | TRP93 |
| B | ARG96 |
| B | LEU100 |
| B | ASN103 |
| B | PRO107 |
| B | GLU113 |
| B | MET114 |
| B | GLN163 |
| B | LYS265 |
| B | HOH573 |
| B | HOH587 |
| B | HOH588 |
| B | HOH596 |
| site_id | AC8 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEC B 403 |
| Chain | Residue |
| B | TYR278 |
| B | MET279 |
| B | HIS280 |
| B | LEU287 |
| B | TYR294 |
| B | SER324 |
| B | GLU327 |
| B | LEU334 |
| B | HOH510 |
| B | HOH548 |
| B | HOH551 |
| B | HOH590 |
| B | HOH595 |
| B | ASN200 |
| B | CYS201 |
| B | CYS204 |
| B | HIS205 |
| B | HIS224 |
| B | LEU228 |
| B | PHE264 |
| B | VAL266 |
| B | PRO267 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 404 |
| Chain | Residue |
| B | LEU75 |
| B | ALA164 |
| B | ARG215 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PO4 B 405 |
| Chain | Residue |
| B | HOH577 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PGE C 201 |
| Chain | Residue |
| C | SER60 |
| C | GLU92 |
| C | GLY93 |
| C | HOH320 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MES D 401 |
| Chain | Residue |
| A | ALA138 |
| D | ARG35 |
| D | LEU37 |
| D | GLU38 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MES F 401 |
| Chain | Residue |
| B | ALA138 |
| B | LEU139 |
| B | GLY141 |
| F | ARG35 |
| F | LEU37 |
| F | GLU38 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA F 402 |
| Chain | Residue |
| F | ASP253 |
| F | SER256 |
| F | ASP258 |
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 |
