3PXS
Crystal Structure of Diferrous MauG in Complex with Pre-Methylamine Dehydrogenase:
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 | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 374 |
| Chain | Residue |
| A | ASN231 |
| A | THR233 |
| A | HOH418 |
| A | HOH426 |
| A | HOH686 |
| A | HOH808 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 375 |
| Chain | Residue |
| A | HOH727 |
| A | HOH973 |
| A | HOH1052 |
| A | LEU250 |
| A | ARG252 |
| A | ILE255 |
| site_id | AC3 |
| Number of Residues | 23 |
| 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 | GLU113 |
| A | MET114 |
| A | GLN163 |
| A | LYS265 |
| A | HOH452 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEC A 600 |
| Chain | Residue |
| A | ASN200 |
| A | CYS201 |
| A | CYS204 |
| A | HIS205 |
| A | HIS224 |
| A | LEU228 |
| A | PHE264 |
| A | PRO267 |
| A | LEU269 |
| A | MET279 |
| A | HIS280 |
| A | LEU287 |
| A | TYR294 |
| A | SER324 |
| A | HOH386 |
| A | HOH415 |
| A | HOH434 |
| A | HOH436 |
| A | HOH448 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 400 |
| Chain | Residue |
| A | ASN66 |
| A | THR275 |
| A | PRO277 |
| A | HOH386 |
| A | HOH399 |
| A | HOH417 |
| A | HOH434 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 374 |
| Chain | Residue |
| B | ASN231 |
| B | THR233 |
| B | HOH391 |
| B | HOH888 |
| B | HOH944 |
| B | HOH945 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 375 |
| Chain | Residue |
| B | LEU250 |
| B | ARG252 |
| B | ILE255 |
| B | HOH420 |
| B | HOH713 |
| B | HOH748 |
| site_id | AC8 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEC B 500 |
| Chain | Residue |
| B | GLN29 |
| B | SER30 |
| B | CYS31 |
| B | CYS34 |
| B | HIS35 |
| B | ARG65 |
| B | THR67 |
| B | PRO68 |
| B | LEU70 |
| B | GLN91 |
| B | PHE92 |
| B | TRP93 |
| B | ARG96 |
| B | LEU100 |
| B | GLN103 |
| B | ALA104 |
| B | PRO107 |
| B | GLU113 |
| B | GLN163 |
| B | LYS265 |
| B | HOH898 |
| B | HOH947 |
| site_id | AC9 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEC B 600 |
| Chain | Residue |
| B | HIS224 |
| B | LEU228 |
| B | PHE264 |
| B | PRO267 |
| B | TYR278 |
| B | MET279 |
| B | HIS280 |
| B | LEU287 |
| B | TYR294 |
| B | SER324 |
| B | HOH395 |
| B | HOH404 |
| B | HOH436 |
| B | HOH444 |
| B | HOH758 |
| B | ASN200 |
| B | CYS201 |
| B | CYS204 |
| B | HIS205 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 400 |
| Chain | Residue |
| B | ASN66 |
| B | THR275 |
| B | PRO277 |
| B | HOH377 |
| B | HOH395 |
| B | HOH404 |
| B | HOH806 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT C 138 |
| Chain | Residue |
| C | SER60 |
| C | GLU92 |
| C | GLY93 |
| D | TRP304 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT D 387 |
| Chain | Residue |
| D | ARG35 |
| D | LEU37 |
| D | GLU38 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PG4 F 387 |
| Chain | Residue |
| F | THR187 |
| F | GLN235 |
| F | LYS236 |
| F | SER255 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PG6 F 388 |
| Chain | Residue |
| A | ARG125 |
| A | ASP128 |
| F | PHE261 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT F 389 |
| Chain | Residue |
| F | ARG35 |
| F | GLU38 |
| F | HOH987 |
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_FI3 |
| 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 | 0AF57 | 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 | 0AF57 | 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 |
