6L8Z
Crystal structure of ugt transferase mutant in complex with UPG
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008194 | molecular_function | UDP-glycosyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | binding site for residue UPG A 501 |
| Chain | Residue |
| A | GLN134 |
| A | TRP351 |
| A | ASN352 |
| A | SER353 |
| A | GLU356 |
| A | ASP372 |
| A | GLN373 |
| A | HOH605 |
| A | HOH636 |
| A | TYR247 |
| A | GLY277 |
| A | SER278 |
| A | VAL304 |
| A | CYS331 |
| A | GLN333 |
| A | HIS348 |
| A | GLY350 |
Functional Information from PROSITE/UniProt
| site_id | PS00375 |
| Number of Residues | 44 |
| Details | UDPGT UDP-glycosyltransferases signature. WcsQleVLahpsvgCFFTHCGwnStleALclgv.PVvafPqwaDQ |
| Chain | Residue | Details |
| A | TRP330-GLN373 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"A0A0A1HA03","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Charge relay","evidences":[{"source":"UniProtKB","id":"A0A0A1HA03","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P51094","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2020","firstPage":"3629","lastPage":"3639","volume":"10","journal":"ACS Catal.","title":"Efficient O-glycosylation of triterpenes enabled by protein engineering of plant glycosyltransferase UGT74AC1.","authors":["Li J.","Yang J.G.","Mu S.","Shang N.","Liu C.","Zhu Y.","Cai Y.","Liu P.","Lin J.","Liu W.D.","Sun Y.X.","Ma Y."],"citationCrossReferences":[{"database":"DOI","id":"10.1021/acscatal.9b05232"}]}},{"source":"PDB","id":"6L8Z","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
