4F97
Crystal Structure of VldE, the pseudo-glycosyltransferase, in complex with GDP and validoxylamine A 7'-phosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004805 | molecular_function | trehalose-phosphatase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0005946 | cellular_component | alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) |
| A | 0005992 | biological_process | trehalose biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016758 | molecular_function | hexosyltransferase activity |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0034605 | biological_process | cellular response to heat |
| A | 0070413 | biological_process | trehalose metabolism in response to stress |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004805 | molecular_function | trehalose-phosphatase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0005946 | cellular_component | alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) |
| B | 0005992 | biological_process | trehalose biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016758 | molecular_function | hexosyltransferase activity |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0034605 | biological_process | cellular response to heat |
| B | 0070413 | biological_process | trehalose metabolism in response to stress |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE GDP A 501 |
| Chain | Residue |
| A | ARG290 |
| A | ASN386 |
| A | LEU387 |
| A | SER388 |
| A | GLU391 |
| A | VDO502 |
| A | HOH645 |
| A | HOH674 |
| A | HOH676 |
| A | HOH683 |
| A | HOH689 |
| A | LYS295 |
| A | HOH706 |
| A | ARG321 |
| A | ASN323 |
| A | ASP360 |
| A | ASN361 |
| A | ASP362 |
| A | VAL363 |
| A | THR366 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE VDO A 502 |
| Chain | Residue |
| A | ASP158 |
| A | HIS182 |
| A | ILE183 |
| A | ARG290 |
| A | ASN325 |
| A | ARG326 |
| A | ASP383 |
| A | GLY384 |
| A | GLN385 |
| A | ASN386 |
| A | GDP501 |
| A | HOH804 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 503 |
| Chain | Residue |
| A | ARG218 |
| A | TRP219 |
| A | GLU406 |
| A | THR407 |
| A | CYS408 |
| A | GLU412 |
| A | HOH714 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 504 |
| Chain | Residue |
| A | TYR110 |
| A | SER187 |
| B | ARG114 |
| B | CL504 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE VDO B 501 |
| Chain | Residue |
| B | ASP158 |
| B | HIS182 |
| B | ILE183 |
| B | PHE215 |
| B | ARG290 |
| B | ASN325 |
| B | ARG326 |
| B | ASP383 |
| B | GLY384 |
| B | GLN385 |
| B | ASN386 |
| B | GDP502 |
| B | HOH740 |
| B | HOH770 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE GDP B 502 |
| Chain | Residue |
| B | ARG290 |
| B | LYS295 |
| B | ARG321 |
| B | ASN323 |
| B | ASP360 |
| B | ASN361 |
| B | ASP362 |
| B | VAL363 |
| B | THR366 |
| B | ASN386 |
| B | LEU387 |
| B | SER388 |
| B | GLU391 |
| B | VDO501 |
| B | HOH659 |
| B | HOH667 |
| B | HOH684 |
| B | HOH692 |
| B | HOH693 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 503 |
| Chain | Residue |
| B | ARG218 |
| B | TRP219 |
| B | GLU406 |
| B | THR407 |
| B | CYS408 |
| B | GLU412 |
| B | HOH617 |
| B | HOH672 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 504 |
| Chain | Residue |
| A | ARG114 |
| A | CL504 |
| B | TYR110 |
| B | SER187 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:23028689, ECO:0007744|PDB:4F97 |
| Chain | Residue | Details |
| A | ASN325 | |
| B | ASP158 | |
| B | HIS182 | |
| B | ASN325 | |
| A | ASP158 | |
| A | HIS182 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:23028689, ECO:0007744|PDB:4F96, ECO:0007744|PDB:4F97, ECO:0007744|PDB:4F9F |
| Chain | Residue | Details |
| A | ASN361 | |
| A | THR366 | |
| A | LEU387 | |
| A | GLU391 | |
| B | ARG290 | |
| B | LYS295 | |
| B | ASN361 | |
| B | THR366 | |
| B | LEU387 | |
| B | GLU391 | |
| A | ARG290 | |
| A | LYS295 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:23028689, ECO:0007744|PDB:4F97, ECO:0007744|PDB:4F9F |
| Chain | Residue | Details |
| A | ARG321 | |
| A | ASP383 | |
| B | ARG321 | |
| B | ASP383 |
