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 | 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 | 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 | 12 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9M9P3 |
Chain | Residue | Details |
A | MET109 | |
B | GLY226 | |
B | ASP257 | |
B | LYS389 | |
A | LYS123 | |
A | GLN199 | |
A | GLY226 | |
A | ASP257 | |
A | LYS389 | |
B | MET109 | |
B | LYS123 | |
B | GLN199 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ASN227 | |
A | LYS421 | |
B | ASN227 | |
B | LYS421 |