6ING
A complex structure of H25A mutant of glycosyltransferase with UDP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008194 | molecular_function | UDP-glycosyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0035251 | molecular_function | UDP-glucosyltransferase activity |
| A | 0080043 | molecular_function | quercetin 3-O-glucosyltransferase activity |
| A | 0080044 | molecular_function | quercetin 7-O-glucosyltransferase activity |
| A | 0102380 | molecular_function | steviolbioside glucosyltransferase activity (rebaudioside B forming) |
| A | 0102381 | molecular_function | stevioside glucosyltransferase activity (rebaudioside A forming) |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | binding site for residue UDP A 501 |
| Chain | Residue |
| A | ASN27 |
| A | SER361 |
| A | GLU364 |
| A | GOL503 |
| A | HOH627 |
| A | HOH654 |
| A | HOH697 |
| A | HOH734 |
| A | HOH777 |
| A | SER283 |
| A | VAL309 |
| A | TRP338 |
| A | VAL339 |
| A | GLN341 |
| A | HIS356 |
| A | TRP359 |
| A | ASN360 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | ARG13 |
| A | LYS39 |
| A | GLY40 |
| A | VAL452 |
| A | SER456 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | GLY24 |
| A | THR146 |
| A | SER147 |
| A | GLY358 |
| A | TRP359 |
| A | ASN360 |
| A | ASP380 |
| A | UDP501 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | SER375 |
| A | ASP376 |
| A | LEU398 |
| A | GLU399 |
| A | ASN400 |
| A | GLY401 |
| A | HOH685 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"31182573","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31324778","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Charge relay","evidences":[{"source":"PubMed","id":"31182573","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31324778","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31324778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6INH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31182573","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31324778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6INF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6O86","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31182573","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31324778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6INI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6O88","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31182573","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31324778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6INI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6KVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6O88","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
