4R16
Structure of UDP-D-MAnNAc dehdrogeanse from Pyrococcus horikoshii
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000271 | biological_process | polysaccharide biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0016628 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor |
| A | 0051287 | molecular_function | NAD binding |
| A | 0089714 | molecular_function | UDP-N-acetyl-D-mannosamine dehydrogenase activity |
| B | 0000271 | biological_process | polysaccharide biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0016628 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor |
| B | 0051287 | molecular_function | NAD binding |
| B | 0089714 | molecular_function | UDP-N-acetyl-D-mannosamine dehydrogenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE SAJ A 501 |
| Chain | Residue |
| A | ILE11 |
| A | ILE215 |
| A | HIS248 |
| A | THR249 |
| A | GLY253 |
| A | VAL254 |
| A | GLY255 |
| A | CYS258 |
| A | LEU259 |
| A | TYR318 |
| A | LYS319 |
| A | ARG152 |
| A | ARG398 |
| A | HOH604 |
| A | HOH607 |
| A | HOH617 |
| A | HOH683 |
| A | HOH816 |
| A | HOH901 |
| A | HOH968 |
| A | HOH969 |
| A | HOH970 |
| A | VAL153 |
| A | HOH978 |
| B | HIS242 |
| B | ARG244 |
| B | VAL245 |
| A | MSE154 |
| A | PRO155 |
| A | LYS204 |
| A | GLU207 |
| A | ASN208 |
| A | ARG211 |
| site_id | AC2 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE SAJ B 501 |
| Chain | Residue |
| A | HIS242 |
| A | ARG244 |
| B | ARG152 |
| B | VAL153 |
| B | MSE154 |
| B | PRO155 |
| B | LYS204 |
| B | GLU207 |
| B | ASN208 |
| B | ARG211 |
| B | ILE215 |
| B | HIS248 |
| B | THR249 |
| B | GLY253 |
| B | VAL254 |
| B | GLY255 |
| B | CYS258 |
| B | LEU259 |
| B | TYR318 |
| B | LYS319 |
| B | ARG398 |
| B | HOH601 |
| B | HOH631 |
| B | HOH647 |
| B | HOH671 |
| B | HOH698 |
| B | HOH716 |
| B | HOH903 |
| B | HOH914 |
| B | HOH977 |
| B | HOH978 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"25305481","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"25305481","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"description":"in chain A","evidences":[{"source":"UniProtKB","id":"P11759","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 18 |
| Details | Binding site: {"description":"in chain A","evidences":[{"source":"PubMed","id":"25305481","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4R16","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"in chain B","evidences":[{"source":"PubMed","id":"25305481","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4R16","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"in chain B","evidences":[{"source":"UniProtKB","id":"P11759","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
