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Structure paper

TitleComparison of human poly-N-acetyl-lactosamine synthase structure with GT-A fold glycosyltransferases supports a modular assembly of catalytic subsites.
Journal, issue, pagesJ. Biol. Chem., Vol. 296, Page 100110-100110, Year 2020
Publish dateApr 21, 2020 (structure data deposition date)
AuthorsKadirvelraj, R. / Yang, J.Y. / Kim, H.W. / Sanders, J.H. / Moremen, K.W. / Wood, Z.A.
External linksJ. Biol. Chem. / PubMed:33229435
MethodsX-ray diffraction
Resolution1.548 - 2.04 Å
Structure data

PDB-6wmm:
Human poly-N-acetyl-lactosamine synthase structure demonstrates a modular assembly of catalytic subsites for GT-A glycosyltransferases
Method: X-RAY DIFFRACTION / Resolution: 1.548 Å

PDB-6wmn:
Human poly-N-acetyl-lactosamine synthase structure demonstrates a modular assembly of catalytic subsites for GT-A glycosyltransferases
Method: X-RAY DIFFRACTION / Resolution: 2.04 Å

PDB-6wmo:
Human poly-N-acetyl-lactosamine synthase structure demonstrates a modular assembly of catalytic subsites for GT-A glycosyltransferases
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-UDP:
URIDINE-5'-DIPHOSPHATE / UDP*YM

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-EPE:
4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / pH buffer*YM

ChemComp-HOH:
WATER

ChemComp-CL:
Unknown entry

ChemComp-GOL:
GLYCEROL

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / Glycosyltransferase / GT-A fold / poly LacNAc synthesis

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