1I12
CRYSTAL STRUCTURE OF SACCHAROMYCES CEREVISIAE GNA1 COMPLEXED WITH ACCOA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004343 | molecular_function | glucosamine 6-phosphate N-acetyltransferase activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| B | 0004343 | molecular_function | glucosamine 6-phosphate N-acetyltransferase activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| C | 0004343 | molecular_function | glucosamine 6-phosphate N-acetyltransferase activity |
| C | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
| C | 0016746 | molecular_function | acyltransferase activity |
| C | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| D | 0004343 | molecular_function | glucosamine 6-phosphate N-acetyltransferase activity |
| D | 0005634 | cellular_component | nucleus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
| D | 0016746 | molecular_function | acyltransferase activity |
| D | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE ACO B 1200 |
| Chain | Residue |
| A | LYS141 |
| B | GLY108 |
| B | GLN109 |
| B | GLY110 |
| B | LEU111 |
| B | GLY112 |
| B | LYS113 |
| B | ASP134 |
| B | ASN139 |
| B | PHE142 |
| B | TYR143 |
| A | ACO1201 |
| B | LYS145 |
| B | HOH1201 |
| B | HOH1238 |
| B | HOH1243 |
| B | HOH1247 |
| B | HOH1249 |
| B | HOH1250 |
| B | HOH1259 |
| B | HOH1266 |
| B | HOH1298 |
| A | HOH1210 |
| B | HOH1306 |
| D | THR29 |
| B | LEU27 |
| B | ASP99 |
| B | ILE100 |
| B | ALA101 |
| B | VAL102 |
| B | GLN107 |
| site_id | AC2 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE ACO A 1201 |
| Chain | Residue |
| A | VAL26 |
| A | LEU27 |
| A | ASP99 |
| A | ILE100 |
| A | ALA101 |
| A | VAL102 |
| A | GLN107 |
| A | GLY108 |
| A | GLN109 |
| A | GLY110 |
| A | LEU111 |
| A | GLY112 |
| A | LYS113 |
| A | ASP134 |
| A | ASN139 |
| A | LYS141 |
| A | PHE142 |
| A | TYR143 |
| A | LYS145 |
| A | HOH1202 |
| A | HOH1228 |
| A | HOH1236 |
| A | HOH1249 |
| A | HOH1262 |
| A | HOH1263 |
| A | HOH1274 |
| A | HOH1286 |
| A | HOH1288 |
| A | HOH1306 |
| A | HOH1333 |
| A | HOH1378 |
| B | LYS141 |
| B | ACO1200 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE ACO C 1202 |
| Chain | Residue |
| C | ASP99 |
| C | ILE100 |
| C | ALA101 |
| C | VAL102 |
| C | GLN107 |
| C | GLY108 |
| C | GLN109 |
| C | GLY110 |
| C | LEU111 |
| C | GLY112 |
| C | LYS113 |
| C | ASP134 |
| C | LYS138 |
| C | ASN139 |
| C | LYS141 |
| C | PHE142 |
| C | TYR143 |
| C | LYS145 |
| C | HOH1205 |
| C | HOH1249 |
| C | HOH1250 |
| C | HOH1258 |
| C | HOH1283 |
| C | HOH1298 |
| C | HOH1312 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ACO D 1203 |
| Chain | Residue |
| D | GLY112 |
| D | LYS113 |
| D | ASP134 |
| D | LYS138 |
| D | ASN139 |
| D | LYS141 |
| D | PHE142 |
| D | TYR143 |
| D | LYS145 |
| D | HOH1207 |
| D | HOH1253 |
| D | VAL26 |
| D | ASP99 |
| D | ILE100 |
| D | ALA101 |
| D | VAL102 |
| D | GLN107 |
| D | GLY108 |
| D | GLN109 |
| D | GLY110 |
| D | LEU111 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE IMD B 1001 |
| Chain | Residue |
| B | ASP117 |
| B | VAL120 |
| B | HOH1258 |
| D | ILE157 |
| D | LYS159 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE IMD A 1002 |
| Chain | Residue |
| A | ILE82 |
| A | HIS96 |
| C | ILE82 |
| C | HIS96 |
| C | HOH1270 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:11278591 |
| Chain | Residue | Details |
| A | THR28 | |
| B | TYR129 | |
| B | ASP134 | |
| B | ARG158 | |
| C | THR28 | |
| C | LYS86 | |
| C | GLU98 | |
| C | TYR129 | |
| C | ASP134 | |
| C | ARG158 | |
| D | THR28 | |
| A | LYS86 | |
| D | LYS86 | |
| D | GLU98 | |
| D | TYR129 | |
| D | ASP134 | |
| D | ARG158 | |
| A | GLU98 | |
| A | TYR129 | |
| A | ASP134 | |
| A | ARG158 | |
| B | THR28 | |
| B | LYS86 | |
| B | GLU98 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11278591, ECO:0007744|PDB:1I12 |
| Chain | Residue | Details |
| A | ILE100 | |
| D | ILE100 | |
| D | GLY108 | |
| D | TYR143 | |
| A | GLY108 | |
| A | TYR143 | |
| B | ILE100 | |
| B | GLY108 | |
| B | TYR143 | |
| C | ILE100 | |
| C | GLY108 | |
| C | TYR143 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: N-acetylserine => ECO:0007744|PubMed:22814378 |
| Chain | Residue | Details |
| A | SER2 | |
| B | SER2 | |
| C | SER2 | |
| D | SER2 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ygh |
| Chain | Residue | Details |
| A | HIS96 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ygh |
| Chain | Residue | Details |
| B | HIS96 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ygh |
| Chain | Residue | Details |
| C | HIS96 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ygh |
| Chain | Residue | Details |
| D | HIS96 |
