1LRW
Crystal structure of methanol dehydrogenase from P. denitrificans
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005509 | molecular_function | calcium ion binding |
A | 0016020 | cellular_component | membrane |
A | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
B | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
B | 0015945 | biological_process | methanol metabolic process |
B | 0015946 | biological_process | methanol oxidation |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0042597 | cellular_component | periplasmic space |
B | 0052933 | molecular_function | alcohol dehydrogenase (cytochrome c(L)) activity |
C | 0005509 | molecular_function | calcium ion binding |
C | 0016020 | cellular_component | membrane |
C | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
C | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
D | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
D | 0015945 | biological_process | methanol metabolic process |
D | 0015946 | biological_process | methanol oxidation |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0042597 | cellular_component | periplasmic space |
D | 0052933 | molecular_function | alcohol dehydrogenase (cytochrome c(L)) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA A 702 |
Chain | Residue |
A | GLU177 |
A | ASN261 |
A | ASP303 |
A | PQQ701 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA C 702 |
Chain | Residue |
C | GLU177 |
C | ASN261 |
C | PQQ701 |
site_id | AC3 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE PQQ A 701 |
Chain | Residue |
A | CYS104 |
A | VAL107 |
A | ARG109 |
A | THR159 |
A | SER174 |
A | GLY175 |
A | ALA176 |
A | GLU177 |
A | THR241 |
A | TRP243 |
A | ARG331 |
A | TRP476 |
A | GLY539 |
A | TRP540 |
A | CA702 |
A | HOH726 |
A | HOH820 |
A | GLU55 |
A | CYS103 |
site_id | AC4 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE PQQ C 701 |
Chain | Residue |
C | GLU55 |
C | CYS103 |
C | ARG109 |
C | THR159 |
C | SER174 |
C | GLY175 |
C | ALA176 |
C | GLU177 |
C | THR241 |
C | TRP243 |
C | ASN261 |
C | ARG331 |
C | TRP476 |
C | GLY539 |
C | TRP540 |
C | CA702 |
C | HOH771 |
C | HOH772 |
C | HOH863 |
Functional Information from PROSITE/UniProt
site_id | PS00363 |
Number of Residues | 29 |
Details | BACTERIAL_PQQ_1 Bacterial quinoprotein dehydrogenases signature 1. NWvmtGRdynaqnYSemtdINkeNVkqLR |
Chain | Residue | Details |
A | ASN13-ARG41 |
site_id | PS00364 |
Number of Residues | 22 |
Details | BACTERIAL_PQQ_2 Bacterial quinoprotein dehydrogenases signature 2. WgwyaYDpevDLFYYgsGnpAP |
Chain | Residue | Details |
A | TRP243-PRO264 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | ASP303 | |
C | ASP303 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | GLU177 | |
A | ASN261 | |
C | GLU177 | |
C | ASN261 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1g72 |
Chain | Residue | Details |
A | ASP303 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1g72 |
Chain | Residue | Details |
C | ASP303 |