2DPH
Crystal Structure of Formaldehyde dismutase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0047895 | molecular_function | formaldehyde dismutase activity |
B | 0000166 | molecular_function | nucleotide binding |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0047895 | molecular_function | formaldehyde dismutase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE NAD A 1403 |
Chain | Residue |
A | GLY46 |
A | ASP217 |
A | GLN218 |
A | ARG222 |
A | LEU236 |
A | ALA261 |
A | VAL262 |
A | HIS267 |
A | PRO298 |
A | ILE300 |
A | ALA337 |
A | SER47 |
A | HOH1411 |
A | HOH1427 |
A | HOH1453 |
A | HOH1454 |
A | HOH1532 |
A | HOH1539 |
A | HIS50 |
A | PHE92 |
A | ASP169 |
A | THR173 |
A | GLY193 |
A | GLY195 |
A | VAL197 |
site_id | AC2 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE NAD B 2403 |
Chain | Residue |
B | GLY46 |
B | SER47 |
B | HIS50 |
B | PHE92 |
B | ASP169 |
B | THR173 |
B | GLY193 |
B | GLY195 |
B | PRO196 |
B | VAL197 |
B | ASP217 |
B | GLN218 |
B | ARG222 |
B | LEU236 |
B | ALA261 |
B | VAL262 |
B | HIS267 |
B | PRO298 |
B | ILE300 |
B | ALA337 |
B | HOH2406 |
B | HOH2451 |
B | HOH2501 |
B | HOH2522 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 1001 |
Chain | Residue |
A | CYS96 |
A | CYS99 |
A | CYS102 |
A | CYS110 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN A 1002 |
Chain | Residue |
A | CYS45 |
A | HIS66 |
A | ASP169 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 1003 |
Chain | Residue |
B | CYS96 |
B | CYS99 |
B | CYS102 |
B | CYS110 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN B 1004 |
Chain | Residue |
B | CYS45 |
B | HIS66 |
B | ASP169 |
Functional Information from PROSITE/UniProt
site_id | PS00059 |
Number of Residues | 15 |
Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEiTGEvvekGsdV |
Chain | Residue | Details |
A | GLY65-VAL79 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 44 |
Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2002","firstPage":"C102","lastPage":"C102","volume":"58","journal":"Acta Crystallogr. A","title":"The X-ray crystal structure of formaldehyde dismutase at 2.3 A resolution.","authors":["Hasegawa T.","Yamano A.","Miura K.","Katsube Y.","Yanase H.","Kato N."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1guf |
Chain | Residue | Details |
A | PHE56 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1guf |
Chain | Residue | Details |
B | PHE56 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1guf |
Chain | Residue | Details |
A | SER47 | |
A | HIS50 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1guf |
Chain | Residue | Details |
B | SER47 | |
B | HIS50 |