Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005507 | molecular_function | copper ion binding |
A | 0009055 | molecular_function | electron transfer activity |
A | 0042597 | cellular_component | periplasmic space |
A | 0046872 | molecular_function | metal ion binding |
C | 0005506 | molecular_function | iron ion binding |
C | 0009055 | molecular_function | electron transfer activity |
C | 0015945 | biological_process | methanol metabolic process |
C | 0020037 | molecular_function | heme binding |
C | 0042597 | cellular_component | periplasmic space |
C | 0046872 | molecular_function | metal ion binding |
H | 0016491 | molecular_function | oxidoreductase activity |
H | 0030058 | molecular_function | amine dehydrogenase activity |
H | 0030416 | biological_process | methylamine metabolic process |
H | 0042597 | cellular_component | periplasmic space |
H | 0052876 | molecular_function | methylamine dehydrogenase (amicyanin) activity |
L | 0009308 | biological_process | amine metabolic process |
L | 0016491 | molecular_function | oxidoreductase activity |
L | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
L | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
L | 0042597 | cellular_component | periplasmic space |
L | 0052876 | molecular_function | methylamine dehydrogenase (amicyanin) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU A 0 |
Chain | Residue |
A | CYS92 |
A | HIS95 |
A | MET98 |
A | HIS53 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PO4 H 0 |
Chain | Residue |
H | LYS341 |
H | HIS362 |
H | HIS362 |
site_id | AC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE HEC C 200 |
Chain | Residue |
C | MET56 |
C | CYS57 |
C | CYS60 |
C | HIS61 |
C | PRO71 |
C | TRP78 |
C | THR79 |
C | TYR80 |
C | ASN83 |
C | LEU89 |
C | THR92 |
C | LEU93 |
C | ALA97 |
C | THR98 |
C | GLN100 |
C | MET101 |
C | MET104 |
site_id | COP |
Number of Residues | 5 |
Details | |
Chain | Residue |
A | CU0 |
H | GLY53 |
H | GLY92 |
H | THR95 |
H | VAL98 |
site_id | HEM |
Number of Residues | 1 |
Details | |
site_id | TTQ |
Number of Residues | 2 |
Details | |
Chain | Residue |
H | ARG57 |
H | PRO108 |
Functional Information from PROSITE/UniProt
site_id | PS00196 |
Number of Residues | 14 |
Details | COPPER_BLUE Type-1 copper (blue) proteins signature. AgtYdYHCt.P.Hpf..M |
Chain | Residue | Details |
A | ALA85-MET98 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: covalent |
Chain | Residue | Details |
C | CYS57 | |
C | CYS60 | |
A | HIS95 | |
A | MET98 | |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
C | HIS61 | |
L | TRP108 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 13 |
Chain | Residue | Details |
L | ASP32 | electrostatic stabiliser, proton acceptor, proton donor |
L | TRQ57 | proton acceptor, proton donor, proton relay |
L | ASP76 | electrostatic stabiliser, proton acceptor, proton donor |
L | TRP108 | proton acceptor, proton donor, proton relay, single electron donor |
L | TYR119 | steric role |
L | THR122 | electrostatic stabiliser |