3U0X
Crystal structure of the B-specific-1,3-galactosyltransferase (GTB) in complex with compound 382
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 | 9 |
Details | BINDING SITE FOR RESIDUE GTI A 1 |
Chain | Residue |
A | ASP211 |
A | ASP213 |
A | MET214 |
A | PRO234 |
A | SER235 |
A | MET266 |
A | LEU324 |
A | ASP326 |
A | GOL356 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 355 |
Chain | Residue |
A | PHE244 |
A | ARG248 |
A | LYS258 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 2 |
Chain | Residue |
A | ARG68 |
B | GLN286 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 356 |
Chain | Residue |
A | GTI1 |
A | HIS233 |
A | PHE236 |
A | THR245 |
A | TRP300 |
A | GLU303 |
A | HOH381 |
A | HOH389 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 357 |
Chain | Residue |
A | GLN253 |
A | ALA254 |
A | ALA287 |
A | HIS305 |
A | LYS308 |
A | HOH487 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 5 |
Chain | Residue |
A | ASP326 |
A | GLN328 |
A | PRO345 |
A | HOH485 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 6 |
Chain | Residue |
A | ASN294 |
A | GLY295 |
A | HOH476 |
B | GLU242 |
B | PHE244 |
B | ARG248 |
B | LYS258 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 358 |
Chain | Residue |
A | LYS82 |
A | PRO333 |
A | ALA334 |
A | HOH361 |
A | HOH407 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 3 |
Chain | Residue |
A | GLN169 |
A | SER171 |
A | ARG199 |
A | HOH398 |
A | HOH458 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 359 |
Chain | Residue |
A | HIS140 |
A | HIS140 |
A | VAL143 |
A | HIS219 |
A | HOH362 |
A | HOH491 |
A | HOH505 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 9 |
Chain | Residue |
A | ARG249 |
A | GLY295 |
A | ILE296 |
A | GLU297 |
B | LYS258 |
site_id | BC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GTI B 1 |
Chain | Residue |
B | ASP211 |
B | ASP213 |
B | MET214 |
B | SER235 |
B | MET266 |
B | LEU324 |
B | ASP326 |
B | LEU329 |
B | LEU330 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 3 |
Chain | Residue |
B | HIS233 |
B | PHE236 |
B | THR245 |
B | TRP300 |
B | GLU303 |
B | HOH408 |
site_id | BC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 4 |
Chain | Residue |
B | GLN253 |
B | ALA254 |
B | ALA287 |
B | HIS305 |
B | LYS308 |
B | TYR309 |
B | HOH467 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 2 |
Chain | Residue |
B | SER171 |
B | ARG199 |
B | HOH430 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 355 |
Chain | Residue |
B | LYS139 |
B | HIS140 |
B | VAL143 |
B | HIS219 |
B | HOH414 |
site_id | BC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 B 12 |
Chain | Residue |
B | HOH43 |
B | PHE121 |
B | ARG188 |
B | ILE192 |
B | CYS209 |
B | GLY267 |
B | PHE270 |
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 |