2VFZ
CRYSTAL STRUCTURE OF ALPHA-1,3 GALACTOSYLTRANSFERASE (R365K) IN COMPLEX WITH UDP-2F-GALACTOSE
Replaces: 2JCFFunctional 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 | 17 |
| Details | BINDING SITE FOR RESIDUE UPF A1360 |
| Chain | Residue |
| A | PHE134 |
| A | HIS280 |
| A | ALA281 |
| A | ALA282 |
| A | HIS315 |
| A | ASP316 |
| A | GLU317 |
| A | LYS359 |
| A | MN1361 |
| A | VAL136 |
| A | TYR139 |
| A | ILE198 |
| A | SER199 |
| A | ARG202 |
| A | ASP225 |
| A | VAL226 |
| A | ASP227 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN A1361 |
| Chain | Residue |
| A | ASP225 |
| A | ASP227 |
| A | UPF1360 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE UPF B2364 |
| Chain | Residue |
| A | PHE92 |
| B | PHE1134 |
| B | ALA1135 |
| B | VAL1136 |
| B | TYR1139 |
| B | TRP1195 |
| B | ILE1198 |
| B | SER1199 |
| B | ARG1202 |
| B | ASP1225 |
| B | VAL1226 |
| B | ASP1227 |
| B | HIS1280 |
| B | ALA1281 |
| B | ALA1282 |
| B | HIS1315 |
| B | ASP1316 |
| B | GLU1317 |
| B | LYS1359 |
| B | HOH2246 |
| B | MN2365 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN B2365 |
| Chain | Residue |
| B | ASP1225 |
| B | ASP1227 |
| B | HOH2247 |
| B | UPF2364 |
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 | 2 |
| Details | Annotated By Reference To The Literature 1g8o |
| Chain | Residue | Details |
| A | GLU317 | |
| A | TRP314 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1g8o |
| Chain | Residue | Details |
| B | GLU1317 | |
| 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 | LYS365 | 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 | LYS1365 | electrostatic stabiliser |
