2JCJ
Crystal structure of alpha-1,3 Galactosyltransferase (C-terminus truncated mutant-C3) in complex with UDP and Tris
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MN A1367 |
Chain | Residue |
A | ASP225 |
A | ASP227 |
A | UDP1366 |
A | HOH2200 |
site_id | AC2 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE UDP A1366 |
Chain | Residue |
A | TYR139 |
A | ILE198 |
A | SER199 |
A | ARG202 |
A | ASP225 |
A | VAL226 |
A | ASP227 |
A | GLU360 |
A | MN1367 |
A | TRS1369 |
A | HOH2097 |
A | HOH2199 |
A | HOH2201 |
A | LYS102 |
A | LYS104 |
A | PHE134 |
A | ALA135 |
A | VAL136 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE TRS A1369 |
Chain | Residue |
A | LYS104 |
A | GLN247 |
A | TYR278 |
A | HIS280 |
A | GLU317 |
A | TRP356 |
A | GLU360 |
A | UDP1366 |
A | HOH2125 |
A | HOH2201 |
A | HOH2202 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MPD A1368 |
Chain | Residue |
A | TYR341 |
A | ILE349 |
A | LYS350 |
A | LEU351 |
A | VAL352 |
A | HOH2189 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A1370 |
Chain | Residue |
A | PRO174 |
A | LEU175 |
A | ILE176 |
A | PHE184 |
A | HOH2203 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:11179209, ECO:0007744|PDB:1G8O |
Chain | Residue | Details |
A | GLU317 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
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 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
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 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
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 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
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 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN293 |
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 | 3 |
Details | Annotated By Reference To The Literature 1g8o |
Chain | Residue | Details |
A | GLU317 | |
A | TRP314 | |
A | ARG365 |
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 |