wwPDB validation report of PDB entry 2VS3

N-ACETYLLACTOSAMINIDE ALPHA-1,3-GALACTOSYLTRANSFERASE

GALACTOSYLTRANSFERASE, UDP-GALACTOSE\: BETA-D-GALACTOSYL-1,4-N-ACETYL-D-GLUCOSAMINIDE ALPHA-1,3-GALACTOSYLTRANSFERASE, ALPHA-1,3 GALACTOSYLTRANSFERASE

ROLES ON INDIVIDUAL RESIDUES OF ALPHA-1,3 GALACTOSYLTRANSFERASES IN SUBSTRATE BINDING AND CATALYSIS

CRYSTAL STRUCTURE OF ALPHA-1,3 GALACTOSYLTRANSFERASE (R365K) IN COMPLEX WITH UDP-2F-GALACTOSE

STRUCTURAL BASIS OF ORDERED BINDING OF DONOR AND ACCEPTOR SUBSTRATES TO THE RETAINING GLYCOSYLTRANSFERASE: ALPHA -1,3 GALACTOSYLTRANSFERASE

ROLES OF ACTIVE SITE TRYPTOPHANS IN SUBSTRATE BINDING AND CATALYSIS BY ALPHA-1, 3 GALACTOSYLTRANSFERASE

ROLES OF INDIVIDUAL RESIDUES OF ALPHA-1,3 GALACTOSYLTRANSFERASES IN SUBSTRATE BINDING AND CATALYSIS

CRYSTAL STRUCTURE OF ALPHA-1,3 GALACTOSYLTRANSFERASE (C-TERMINUS TRUNCATED MUTANT-C3) IN COMPLEX WITH UDP AND TRIS

CRYSTAL STRUCTURE OF ALPHA-1,3 GALACTOSYLTRANSFERASE (R365K) IN COMPLEX WITH UDP AND 2 MANGANESE ION

CRYSTAL STRUCTURE OF THE BOVINE CATALYTIC DOMAIN OF ALPHA-1,3-GALACTOSYLTRANSFERASE IN THE PRESENCE OF UDP-GALACTOSE

CRYSTALLOGRAPHIC STRUCTURE OF THE NATIVE BOVINE ALPHA-1,3-GALACTOSYLTRANSFERASE CATALYTIC DOMAIN

1.53 A CRYSTAL STRUCTURE OF THE BETA- GALACTOSIDE-ALPHA-1,3-GALACTOSYLTRANSFERASE IN COMPLEX WITH UDP

CRYSTAL STRUCTURE OF ALPHA-1,3 GALACTOSYLTRANSFERASE (R365K) IN THE ABSENCE OF LIGANDS

CRYSTAL STRUCTURE OF WILD TYPE ALPHA-1,3 GALACTOSYLTRANSFERASE IN THE ABSENCE OF LIGANDS

CRYSTAL STRUCTURE OF BOVINE ALPHA-1,3- GALACTOSYLTRANSFERASECATALYTIC DOMAIN.

THE BINDING OF UDP-GALACTOSE BY AN ACTIVE SITE MUTANT OF ALPHA-1,3 GALACTOSYLTRANSFERASE (ALPHA3GT)

ENGINEERED RESIDUE IN CHAIN A, ASP 316 TO ASN ENGINEERED RESIDUE IN CHAIN B, ASP 316 TO ASN

N-ACETYLLACTOSAMINIDE ALPHA-1,3-GALACTOSYLTRANSFERASE (E.C.2.4.1.87)

The analyses of the Patterson function reveals a significant off-origin peak that is 35.61 % of the origin peak, indicating pseudo-translational symmetry. The chance of finding a peak of this or larger height by random in a structure without pseudo-translational symmetry is equal to 5.6782e-04. The detected translational NCS is most likely also responsible for the elevated intensity ratio. See the relevant section of the logfile for more details.

20191225.v01 (using entries in the PDB archive December 25th 2019)

structure factor analysis and validation

geometric validation package for ligand chemistry in protein x-ray structures