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 | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:25305481 |
Chain | Residue | Details |
A | LYS204 | |
B | LYS204 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:25305481 |
Chain | Residue | Details |
A | CYS258 | |
B | CYS258 |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | BINDING: in chain A => ECO:0000250|UniProtKB:P11759 |
Chain | Residue | Details |
A | TYR10 | |
B | THR119 | |
A | ILE11 | |
A | ASP30 | |
A | THR85 | |
A | THR119 | |
B | TYR10 | |
B | ILE11 | |
B | ASP30 | |
B | THR85 |
site_id | SWS_FT_FI4 |
Number of Residues | 20 |
Details | BINDING: in chain A => ECO:0000269|PubMed:25305481, ECO:0007744|PDB:4R16 |
Chain | Residue | Details |
A | ARG152 | |
A | ARG398 | |
B | ARG152 | |
B | VAL153 | |
B | LYS204 | |
B | ASN208 | |
B | ARG211 | |
B | THR249 | |
B | GLY255 | |
B | TYR318 | |
B | LYS319 | |
A | VAL153 | |
B | ARG398 | |
A | LYS204 | |
A | ASN208 | |
A | ARG211 | |
A | THR249 | |
A | GLY255 | |
A | TYR318 | |
A | LYS319 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: in chain B => ECO:0000269|PubMed:25305481, ECO:0007744|PDB:4R16 |
Chain | Residue | Details |
A | HIS242 | |
A | ARG244 | |
B | HIS242 | |
B | ARG244 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | BINDING: in chain B => ECO:0000250|UniProtKB:P11759 |
Chain | Residue | Details |
A | LYS261 | |
A | ARG326 | |
B | LYS261 | |
B | ARG326 |