wwPDB validation report of PDB entry 1OC6

N-LINKED N-ACETYLGLUCOSAMINE ON RESIDUE ASN 141

CELLOBIOHYDROLASE II (CEL6A) FROM HUMICOLA INSOLENS

MUTANT D416A OF THE CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS IN COMPLEX WITH METHYL-CELLOBIOSYL-4-DEOXY-4-THIO-BETA-D- CELLOBIOSIDE

STRUCTURE NATIVE OF THE D405N MUTANT OF THE CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS AT 1.5 ANGSTROM RESOLUTION

D405N MUTANT OF THE CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS IN COMPLEX WITH METHYL-TETRATHIO-ALPHA-D-CELLOPENTOSIDE AT 1 .1 ANGSTROM RESOLUTION

STRUCTURE OF THE WILD-TYPE CELLOBIOHYDROLASE CEL6A FROM HUMICOLAS INSOLENS IN COMPLEX WITH A FLUORESCENT SUBSTRATE

MUTANT D416A OF THE CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS IN COMPLEX WITH A THIOPENTASACCHARIDE AT 1.3 ANGSTROM RESOLUTION

MUTANT D416A OF THE CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS IN COMPLEX WITH A CELLOBIO-DERIVED ISOFAGOMINE AT 1.3 ANGSTROM RESOLUTION

CEL6A (Y169F) WITH A NON-HYDROLYSABLE CELLOTETRAOSE

WILD TYPE CEL6A WITH A NON-HYDROLYSABLE CELLOTETRAOSE

CELLOBIOHYDROLASE II (CEL6A) FROM HUMICOLA INSOLENS IN COMPLEX WITH GLUCOSE AND CELLOTETRAOSE

THIS MUTANT HAS BEEN PRODUCED BY SITE DIRECTED MUTAGENESIS.
THE CLONING WAS PERFORMED SUCH AS ONLY THE SIGNAL PEPTIDE
AND THE CATALYTIC DOMAIN WERE EXPRESSED. THE CATALYTIC DOMAIN
SHOULD BEGIN AT PHE 89. OUR NUMBERING BEGIN AT THE FIRST RESIDUE
OF THE MATURE PROTEIN WHICH EXPLAIN A DIFFERENCE WITH THE
DATABASE SEQUENCE WHICH INCLUDE THE PROSEQUENCE. HERE,DUE
TO THE INCORRECT PROCESSING OF THE SIGNAL PEPTIDE ALA 87 AND
PRO 88 ARE ALSO PRESENT IN THE MATURE PROTEIN.

THIS PROTEIN IS CLOSELY RELATED TO AVICELASE 2 (SWISS-PROT
ACCESSION ID:Q9C1S9) WITH WHICH IT HAS 96% SEQUENCE IDENTITY.

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

The largest off-origin peak in the Patterson function is 6.84% of the height of the origin peak. No significant pseudotranslation is detected.

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