3IOJ
Crystal structure of the Fucosylgalactoside alpha N-acetylgalactosaminyltransferase (GTA, cisAB mutant L266G, G268A) in complex with UDP
Functional 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 406 |
Chain | Residue |
A | ASP211 |
A | ASP213 |
A | UDP475 |
A | HOH513 |
site_id | AC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE UDP A 475 |
Chain | Residue |
A | VAL212 |
A | ASP213 |
A | LYS346 |
A | HOH360 |
A | HOH378 |
A | MN406 |
A | HOH496 |
A | HOH500 |
A | HOH513 |
A | HOH561 |
A | PHE121 |
A | ILE123 |
A | TYR126 |
A | ARG188 |
A | ASP211 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 3968 |
Chain | Residue |
A | HOH49 |
A | HIS233 |
A | PHE236 |
A | THR245 |
A | TYR264 |
A | TRP300 |
A | GLU303 |
A | HOH358 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1 |
Chain | Residue |
A | ARG110 |
A | ARG146 |
B | THR166 |
B | GLY167 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 2 |
Chain | Residue |
A | THR166 |
A | GLY167 |
A | HOH491 |
B | ARG110 |
B | ASN113 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 3 |
Chain | Residue |
A | GLN169 |
A | SER171 |
A | ARG199 |
A | ARG279 |
A | ARG282 |
A | HOH551 |
A | HOH574 |
A | HOH577 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MN B 406 |
Chain | Residue |
B | ASP211 |
B | ASP213 |
B | HOH454 |
B | UDP475 |
site_id | AC8 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE UDP B 475 |
Chain | Residue |
B | PHE121 |
B | ALA122 |
B | ILE123 |
B | LYS124 |
B | TYR126 |
B | VAL184 |
B | ARG188 |
B | ASP211 |
B | VAL212 |
B | ASP213 |
B | LYS346 |
B | HOH359 |
B | MN406 |
B | HOH470 |
B | HOH581 |
site_id | AC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 3968 |
Chain | Residue |
B | HIS233 |
B | PHE236 |
B | THR245 |
B | TRP300 |
B | GLU303 |
B | HOH390 |
B | HOH419 |
B | HOH500 |
B | HOH581 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 4 |
Chain | Residue |
B | SER171 |
B | ARG199 |
B | HOH380 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P14769 |
Chain | Residue | Details |
A | GLU303 | |
B | GLU303 |
Chain | Residue | Details |
A | PHE121 | |
B | PHE121 |
Chain | Residue | Details |
A | TYR126 | |
B | TYR126 |
Chain | Residue | Details |
A | ASP211 | |
A | ASP213 | |
B | ASP211 | |
B | ASP213 |
Chain | Residue | Details |
A | HIS233 | |
B | HIS233 |
Chain | Residue | Details |
A | THR245 | |
B | THR245 |
Chain | Residue | Details |
A | GLU303 | |
B | GLU303 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12972418, ECO:0000269|PubMed:16326711, ECO:0007744|PDB:1R7T, ECO:0007744|PDB:1ZI4, ECO:0007744|PDB:1ZI5, ECO:0007744|PDB:1ZJ2, ECO:0007744|PDB:1ZJ3, ECO:0007744|PDB:2RIY, ECO:0007744|PDB:2RJ1, ECO:0007744|PDB:2RJ4, ECO:0007744|PDB:2RJ6, ECO:0007744|PDB:2RJ7, ECO:0007744|PDB:2RJ8, ECO:0007744|PDB:2RJ9, ECO:0007744|PDB:3V0M, ECO:0007744|PDB:3V0O, ECO:0007744|PDB:3V0P, ECO:0007744|PDB:3V0Q, ECO:0007744|PDB:4C2S, ECO:0007744|PDB:4KC1, ECO:0007744|PDB:4KC2, ECO:0007744|PDB:4KC4 |
Chain | Residue | Details |
A | ASP326 | |
B | ASP326 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN113 | |
B | ASN113 |