7CJ4
Crystal structure of homo dimeric D-allulose 3-epimerase from Methylomonas sp.
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue MN A 301 |
Chain | Residue |
A | GLU152 |
A | ASP185 |
A | HIS211 |
A | GLU246 |
A | HOH492 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue MN B 301 |
Chain | Residue |
B | HOH401 |
B | GLU152 |
B | ASP185 |
B | HIS211 |
B | GLU246 |
Functional Information from PROSITE/UniProt
site_id | PS00105 |
Number of Residues | 14 |
Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. GMAKsvLAaGDRLG |
Chain | Residue | Details |
A | GLY195-GLY208 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"Q9WYP7","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"33838083","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7CJ5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7CJ9","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"33838083","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7CJ5","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"7CJ4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7CJ6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7CJ7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7CJ8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7CJ9","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |