2YQJ
Crystal Structure of uridine-diphospho-N-acetylglucosamine pyrophosphorylase from Candida albicans, in the reaction-completed form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003977 | molecular_function | UDP-N-acetylglucosamine diphosphorylase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0019276 | biological_process | UDP-N-acetylgalactosamine metabolic process |
| A | 0052630 | molecular_function | UDP-N-acetylgalactosamine diphosphorylase activity |
| A | 0070569 | molecular_function | uridylyltransferase activity |
| B | 0003977 | molecular_function | UDP-N-acetylglucosamine diphosphorylase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0019276 | biological_process | UDP-N-acetylgalactosamine metabolic process |
| B | 0052630 | molecular_function | UDP-N-acetylgalactosamine diphosphorylase activity |
| B | 0070569 | molecular_function | uridylyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1101 |
| Chain | Residue |
| A | GLY114 |
| A | THR115 |
| A | ARG116 |
| A | UD11001 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1102 |
| Chain | Residue |
| A | ARG285 |
| A | LYS328 |
| A | ARG332 |
| A | HOH1415 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 1201 |
| Chain | Residue |
| A | THR77 |
| A | HOH1445 |
| A | ASN74 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2102 |
| Chain | Residue |
| B | LYS328 |
| B | ARG332 |
| site_id | AC5 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE UD1 A 1001 |
| Chain | Residue |
| A | MET109 |
| A | GLY111 |
| A | GLY112 |
| A | ARG116 |
| A | MET168 |
| A | GLN199 |
| A | PRO224 |
| A | GLY226 |
| A | ASN227 |
| A | CYS255 |
| A | VAL256 |
| A | VAL293 |
| A | GLY294 |
| A | GLU309 |
| A | TYR310 |
| A | ASN335 |
| A | VAL337 |
| A | PHE393 |
| A | PHE395 |
| A | PHE417 |
| A | LYS421 |
| A | SO41101 |
| A | HOH1366 |
| A | HOH1386 |
| A | HOH1389 |
| A | HOH1402 |
| A | HOH1404 |
| A | HOH1439 |
| site_id | AC6 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE UD1 B 2001 |
| Chain | Residue |
| B | MET109 |
| B | GLY111 |
| B | GLY112 |
| B | ARG116 |
| B | MET168 |
| B | GLN199 |
| B | PRO224 |
| B | GLY226 |
| B | ASN227 |
| B | CYS255 |
| B | VAL256 |
| B | ASP257 |
| B | VAL293 |
| B | GLY294 |
| B | GLU309 |
| B | TYR310 |
| B | ASN335 |
| B | VAL337 |
| B | PHE393 |
| B | PHE395 |
| B | PHE417 |
| B | LYS421 |
| B | HOH2114 |
| B | HOH2119 |
| B | HOH2171 |
| B | HOH2175 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1301 |
| Chain | Residue |
| A | PHE196 |
| A | ASN237 |
| A | HOH1313 |
| A | HOH1377 |
| B | GLN6 |
| B | HOH2174 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Motif: {"description":"Substrate binding","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9M9P3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
