4F96
Crystal Structure of VldE, the pseudo-glycosyltransferase, in complex with GDP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003825 | molecular_function | alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity |
| 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 |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003825 | molecular_function | alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE GDP B 501 |
| Chain | Residue |
| B | ARG290 |
| B | LEU387 |
| B | SER388 |
| B | GLU391 |
| B | HOH660 |
| B | HOH675 |
| B | HOH676 |
| B | HOH688 |
| B | HOH706 |
| B | HOH716 |
| B | HOH779 |
| B | LYS295 |
| B | ARG321 |
| B | ASN323 |
| B | ASP360 |
| B | ASN361 |
| B | ASP362 |
| B | THR366 |
| B | ASN386 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 502 |
| Chain | Residue |
| A | ARG114 |
| A | CL502 |
| B | TYR110 |
| B | SER187 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE GDP A 501 |
| Chain | Residue |
| A | ARG290 |
| A | LYS295 |
| A | ARG321 |
| A | ASN323 |
| A | ASP360 |
| A | ASN361 |
| A | ASP362 |
| A | VAL363 |
| A | THR366 |
| A | ASN386 |
| A | LEU387 |
| A | SER388 |
| A | GLU391 |
| A | HOH663 |
| A | HOH677 |
| A | HOH687 |
| A | HOH695 |
| A | HOH722 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 502 |
| Chain | Residue |
| A | TYR110 |
| A | SER187 |
| B | ARG114 |
| B | CL502 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23028689","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4F97","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23028689","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4F96","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4F97","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4F9F","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23028689","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4F97","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4F9F","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
