3PXT
Crystal Structure of Ferrous CO Adduct of 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 | 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 | 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 | 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 | 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 | HOH382 |
A | HOH388 |
A | HOH519 |
A | HOH680 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 375 |
Chain | Residue |
A | HOH436 |
A | HOH865 |
A | HOH1080 |
A | LEU250 |
A | ARG252 |
A | ILE255 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CMO A 376 |
Chain | Residue |
A | PHE92 |
A | GLN103 |
A | PRO107 |
A | HEC500 |
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 | GLU113 |
A | GLN163 |
A | LYS265 |
A | CMO376 |
A | HOH393 |
A | HOH703 |
site_id | AC5 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE HEC A 600 |
Chain | Residue |
A | TRP93 |
A | ASN200 |
A | CYS201 |
A | CYS204 |
A | HIS205 |
A | HIS224 |
A | ILE226 |
A | LEU228 |
A | PHE264 |
A | PRO267 |
A | LEU269 |
A | TYR278 |
A | MET279 |
A | HIS280 |
A | LEU287 |
A | TYR294 |
A | SER324 |
A | HOH394 |
A | HOH395 |
A | HOH406 |
A | HOH408 |
A | HOH428 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A 400 |
Chain | Residue |
A | ASN66 |
A | THR275 |
A | PRO277 |
A | HOH398 |
A | HOH406 |
A | HOH408 |
A | HOH430 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA B 374 |
Chain | Residue |
B | ASN231 |
B | THR233 |
B | HOH437 |
B | HOH440 |
B | HOH444 |
B | HOH974 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CMO B 375 |
Chain | Residue |
B | PHE92 |
B | GLN103 |
B | PRO107 |
B | GLU113 |
B | HEC500 |
site_id | AC9 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE HEC B 500 |
Chain | Residue |
B | CMO375 |
B | HOH502 |
B | HOH632 |
B | HOH750 |
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 | PRO107 |
B | MET114 |
B | GLN163 |
B | LYS265 |
site_id | BC1 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE HEC B 600 |
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 | SER324 |
B | HOH402 |
B | HOH418 |
B | HOH449 |
B | HOH461 |
B | HOH673 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA B 400 |
Chain | Residue |
B | ASN66 |
B | THR275 |
B | PRO277 |
B | HOH379 |
B | HOH402 |
B | HOH405 |
B | HOH461 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT C 138 |
Chain | Residue |
C | SER60 |
C | GLY93 |
D | TRP304 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT D 387 |
Chain | Residue |
D | ARG35 |
D | LEU37 |
D | GLU38 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT F 387 |
Chain | Residue |
F | ARG35 |
F | LEU37 |
F | GLU38 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PG6 F 388 |
Chain | Residue |
A | ARG25 |
A | ASN26 |
A | ARG125 |
A | ASP128 |
F | PHE261 |
F | HOH985 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: Tryptophylquinone => ECO:0000269|PubMed:1409575 |
Chain | Residue | Details |
C | 0AF57 | |
E | 0AF57 | |
A | CYS201 | |
A | CYS204 | |
B | CYS31 | |
B | CYS34 | |
B | CYS201 | |
B | CYS204 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | CROSSLNK: Tryptophan tryptophylquinone (Trp-Trp) => ECO:0000269|PubMed:1409575 |
Chain | Residue | Details |
C | 0AF57 | |
C | TRP108 | |
E | 0AF57 | |
E | TRP108 | |
B | HIS205 | |
B | HIS280 |
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 | ASP76 | electrostatic stabiliser, proton acceptor, proton donor |
C | TRP108 | proton acceptor, proton donor, proton relay, single electron donor |
C | TYR119 | steric role |
C | THR122 | 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 | ASP76 | electrostatic stabiliser, proton acceptor, proton donor |
E | TRP108 | proton acceptor, proton donor, proton relay, single electron donor |
E | TYR119 | steric role |
E | THR122 | electrostatic stabiliser |