1VZT
ROLES OF INDIVIDUAL RESIDUES OF ALPHA-1,3 GALACTOSYLTRANSFERASES IN SUBSTRATE BINDING AND CATALYSIS
Replaces: 1O7RFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016758 | molecular_function | hexosyltransferase activity |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016758 | molecular_function | hexosyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN A 1369 |
| Chain | Residue |
| A | ASP225 |
| A | ASP227 |
| A | UDP1370 |
| A | HOH2211 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN B 2369 |
| Chain | Residue |
| B | ASP1225 |
| B | ASP1227 |
| B | HOH2221 |
| B | UDP2370 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE UDP A 1370 |
| Chain | Residue |
| A | ALA135 |
| A | VAL136 |
| A | TYR139 |
| A | ILE198 |
| A | SER199 |
| A | ARG202 |
| A | ASP225 |
| A | VAL226 |
| A | ASP227 |
| A | LYS359 |
| A | TYR361 |
| A | ARG365 |
| A | MN1369 |
| A | TRS1371 |
| A | HOH2110 |
| A | HOH2211 |
| A | HOH2212 |
| A | HOH2213 |
| A | HOH2214 |
| A | HOH2215 |
| A | HOH2216 |
| A | PHE134 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE TRS A 1371 |
| Chain | Residue |
| A | SER199 |
| A | ALA281 |
| A | TRP314 |
| A | HIS315 |
| A | ASP316 |
| A | GLU317 |
| A | UDP1370 |
| A | HOH2214 |
| A | HOH2215 |
| A | HOH2217 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE UDP B 2370 |
| Chain | Residue |
| B | PHE1134 |
| B | ALA1135 |
| B | VAL1136 |
| B | TYR1139 |
| B | ILE1198 |
| B | SER1199 |
| B | ARG1202 |
| B | ASP1225 |
| B | VAL1226 |
| B | ASP1227 |
| B | LYS1359 |
| B | TYR1361 |
| B | ARG1365 |
| B | HOH2089 |
| B | HOH2093 |
| B | HOH2221 |
| B | HOH2222 |
| B | HOH2223 |
| B | HOH2224 |
| B | HOH2225 |
| B | MN2369 |
| B | TRS2371 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE TRS B 2371 |
| Chain | Residue |
| B | ALA1281 |
| B | TRP1314 |
| B | HIS1315 |
| B | ASP1316 |
| B | GLU1317 |
| B | HOH2090 |
| B | HOH2223 |
| B | HOH2225 |
| B | UDP2370 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:11179209, ECO:0007744|PDB:1G8O |
| Chain | Residue | Details |
| A | GLU317 | |
| B | GLU1317 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11179209, ECO:0000269|PubMed:11592969, ECO:0000269|PubMed:12011052, ECO:0007744|PDB:1G93, ECO:0007744|PDB:1GWV, ECO:0007744|PDB:1GWW, ECO:0007744|PDB:1GX0, ECO:0007744|PDB:1GX4, ECO:0007744|PDB:1K4V, ECO:0007744|PDB:1O7O, ECO:0007744|PDB:1O7Q, ECO:0007744|PDB:1VZT, ECO:0007744|PDB:1VZU, ECO:0007744|PDB:1VZX, ECO:0007744|PDB:2JCK, ECO:0007744|PDB:2VFZ, ECO:0007744|PDB:2VS3, ECO:0007744|PDB:2VS4, ECO:0007744|PDB:2VS5, ECO:0007744|PDB:2VXL, ECO:0007744|PDB:2WGZ |
| Chain | Residue | Details |
| A | PHE134 | |
| B | PHE1134 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11179209, ECO:0000269|PubMed:11592969, ECO:0000269|PubMed:12011052, ECO:0007744|PDB:1G8O, ECO:0007744|PDB:1G93, ECO:0007744|PDB:1GWV, ECO:0007744|PDB:1GWW, ECO:0007744|PDB:1GX0, ECO:0007744|PDB:1GX4, ECO:0007744|PDB:1K4V, ECO:0007744|PDB:1O7O, ECO:0007744|PDB:1O7Q, ECO:0007744|PDB:1VZT, ECO:0007744|PDB:1VZU, ECO:0007744|PDB:1VZX, ECO:0007744|PDB:2JCK, ECO:0007744|PDB:2VFZ, ECO:0007744|PDB:2VS3, ECO:0007744|PDB:2VS4, ECO:0007744|PDB:2VS5, ECO:0007744|PDB:2VXL, ECO:0007744|PDB:2WGZ |
| Chain | Residue | Details |
| A | ASP225 | |
| A | ASP227 | |
| B | ASP1225 | |
| B | ASP1227 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12011052, ECO:0007744|PDB:1GWV, ECO:0007744|PDB:1GX4, ECO:0007744|PDB:1O7O, ECO:0007744|PDB:1O7Q, ECO:0007744|PDB:1VZX, ECO:0007744|PDB:2VS4, ECO:0007744|PDB:2WGZ |
| Chain | Residue | Details |
| A | GLN247 | |
| A | THR259 | |
| B | GLN1247 | |
| B | THR1259 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11592969, ECO:0000269|PubMed:12011052, ECO:0007744|PDB:1GWV, ECO:0007744|PDB:1GWW, ECO:0007744|PDB:1GX0, ECO:0007744|PDB:1GX4, ECO:0007744|PDB:1K4V, ECO:0007744|PDB:1O7O, ECO:0007744|PDB:1O7Q, ECO:0007744|PDB:1VZT, ECO:0007744|PDB:1VZU, ECO:0007744|PDB:1VZX, ECO:0007744|PDB:2JCK, ECO:0007744|PDB:2VFZ, ECO:0007744|PDB:2VS3, ECO:0007744|PDB:2VS4, ECO:0007744|PDB:2VS5, ECO:0007744|PDB:2WGZ |
| Chain | Residue | Details |
| A | LYS359 | |
| B | LYS1359 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN293 | |
| B | ASN1293 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1g8o |
| Chain | Residue | Details |
| A | GLU317 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1g8o |
| Chain | Residue | Details |
| B | GLU1317 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1g8o |
| Chain | Residue | Details |
| A | GLU317 | |
| A | TRP314 | |
| A | ARG365 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1g8o |
| Chain | Residue | Details |
| B | GLU1317 | |
| B | ARG1365 | |
| B | TRP1314 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 356 |
| Chain | Residue | Details |
| A | GLN247 | electrostatic stabiliser, hydrogen bond donor |
| A | HIS280 | electrostatic stabiliser, hydrogen bond donor |
| A | TRP314 | electrostatic stabiliser, hydrogen bond donor |
| A | GLU317 | activator, covalently attached, electrostatic stabiliser, nucleofuge, nucleophile |
| A | TRP356 | electrostatic stabiliser, hydrogen bond donor |
| A | ARG365 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 356 |
| Chain | Residue | Details |
| B | GLN1247 | electrostatic stabiliser, hydrogen bond donor |
| B | HIS1280 | electrostatic stabiliser, hydrogen bond donor |
| B | TRP1314 | electrostatic stabiliser, hydrogen bond donor |
| B | GLU1317 | activator, covalently attached, electrostatic stabiliser, nucleofuge, nucleophile |
| B | TRP1356 | electrostatic stabiliser, hydrogen bond donor |
| B | ARG1365 | electrostatic stabiliser |
