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 |