1MDA
CRYSTAL STRUCTURE OF AN ELECTRON-TRANSFER COMPLEX BETWEEN METHYLAMINE DEHYDROGENASE AND 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 | 0030058 | molecular_function | amine dehydrogenase activity |
H | 0042597 | cellular_component | periplasmic space |
J | 0030058 | molecular_function | amine dehydrogenase activity |
J | 0042597 | cellular_component | periplasmic space |
L | 0009308 | biological_process | amine metabolic process |
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 | 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 0 |
Chain | Residue |
A | HIS53 |
A | CYS92 |
A | HIS95 |
A | MET98 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU B 0 |
Chain | Residue |
B | HIS53 |
B | CYS92 |
B | HIS95 |
B | MET98 |
site_id | CUE |
Number of Residues | 5 |
Details |
Chain | Residue |
A | CU0 |
A | HIS53 |
A | CYS92 |
A | HIS95 |
A | MET98 |
site_id | CUF |
Number of Residues | 5 |
Details |
Chain | Residue |
B | CU0 |
B | HIS53 |
B | CYS92 |
B | HIS95 |
B | MET98 |
site_id | TQB |
Number of Residues | 2 |
Details |
Chain | Residue |
L | TRQ57 |
L | TRP107 |
site_id | TQD |
Number of Residues | 2 |
Details |
Chain | Residue |
M | TRQ57 |
M | TRP107 |
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 | 8 |
Details | BINDING: |
Chain | Residue | Details |
A | HIS53 | |
A | CYS92 | |
A | HIS95 | |
A | MET98 | |
B | HIS53 | |
B | CYS92 | |
B | HIS95 | |
B | MET98 |