2J55
X-ray reduced Paraccocus denitrificans methylamine dehydrogenase O- quinone in complex with amicyanin.
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 |
B | 0005507 | molecular_function | copper ion binding |
B | 0009055 | molecular_function | electron transfer activity |
B | 0042597 | cellular_component | periplasmic space |
B | 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 |
J | 0016491 | molecular_function | oxidoreductase activity |
J | 0030058 | molecular_function | amine dehydrogenase activity |
J | 0030416 | biological_process | methylamine metabolic process |
J | 0042597 | cellular_component | periplasmic space |
J | 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 |
M | 0009308 | biological_process | amine metabolic process |
M | 0016491 | molecular_function | oxidoreductase activity |
M | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
M | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
M | 0042597 | cellular_component | periplasmic space |
M | 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 1106 |
Chain | Residue |
A | HIS53 |
A | CYS92 |
A | HIS95 |
A | MET98 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU B 1106 |
Chain | Residue |
B | HIS53 |
B | CYS92 |
B | HIS95 |
B | MET98 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL H 1387 |
Chain | Residue |
H | HIS250 |
H | LEU262 |
H | ALA264 |
H | HOH2277 |
H | PHE220 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL H 1388 |
Chain | Residue |
H | HIS54 |
H | TRP282 |
H | GLN378 |
H | HOH2392 |
H | HOH2402 |
L | HOH2021 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL H 1389 |
Chain | Residue |
H | GLN14 |
H | ALA18 |
H | ARG70 |
H | HOH2012 |
H | HOH2403 |
H | HOH2405 |
H | HOH2406 |
M | ASP37 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL L 1132 |
Chain | Residue |
H | ARG305 |
L | CYS23 |
L | CYS88 |
L | LEU89 |
L | ASN90 |
L | HOH2048 |
L | HOH2073 |
L | HOH2074 |
L | HOH2075 |
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 | MOD_RES: Tryptophylquinone => ECO:0000269|PubMed:1409575 |
Chain | Residue | Details |
L | TRQ57 | |
M | TRQ57 | |
A | HIS95 | |
A | MET98 | |
B | HIS53 | |
B | CYS92 | |
B | HIS95 | |
B | MET98 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | CROSSLNK: Tryptophan tryptophylquinone (Trp-Trp) => ECO:0000269|PubMed:1409575 |
Chain | Residue | Details |
L | TRQ57 | |
L | TRP108 | |
M | TRQ57 | |
M | TRP108 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 2bbk |
Chain | Residue | Details |
L | ASP76 | |
L | THR122 | |
L | ASP32 | |
L | TYR119 | |
L | TRP108 |
site_id | CSA2 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 2bbk |
Chain | Residue | Details |
M | ASP76 | |
M | THR122 | |
M | ASP32 | |
M | TYR119 | |
M | TRP108 |
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 |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 13 |
Chain | Residue | Details |
M | ASP32 | electrostatic stabiliser, proton acceptor, proton donor |
M | TRQ57 | proton acceptor, proton donor, proton relay |
M | ASP76 | electrostatic stabiliser, proton acceptor, proton donor |
M | TRP108 | proton acceptor, proton donor, proton relay, single electron donor |
M | TYR119 | steric role |
M | THR122 | electrostatic stabiliser |