wwPDB validation report of PDB entry 2Y55

DD-CARBOXYPEPTIDASE, DD-PEPTIDASE, PENICILLIN-BINDING PROTEIN, PBP

CRYSTAL STRUCTURE OF THE DD-TRANSPEPTIDASE- CARBOXYPEPTIDASE FROM ACTINOMADURA R39

CRYSTAL STRUCTURE OF ACTINOMADURA R39 DD- PEPTIDASE COMPLEXED WITH A PEPTIDOGLYCAN- MIMETIC CEPHALOSPORIN

CRYSTAL STRUCTURE OF A COMPLEX BETWEEN ACTINOMADURA R39 DD-PEPTIDASE AND A BORONATE INHIBITOR

CRYSTAL STRUCTURE OF THE NITROCEFIN ACYL-DD -PEPTIDASE FROM ACTINOMADURA R39.

CRYSTAL STRUCTURE OF A COMPLEX BETWEEN ACTINOMADURA R39 DD-PEPTIDASE AND A PEPTIDOGLYCAN MIMETIC BORONATE INHIBITOR

CRYSTAL STRUCTURE OF THE ACTINOMADURA R39 DD -PEPTIDASE INHIBITED BY 6-BETA- IODOPENICILLANATE.

CRYSTAL STRUCTURE OF THE DD-PEPTIDASE FROM ACTINOMADURA R39 WITH COBALT IONS

UNEXPECTED TRICOVALENT BINDING MODE OF BORONIC ACIDS WITHIN THE ACTIVE SITE OF A PENICILLIN BINDING PROTEIN

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.

D-ALANYL-D-ALANINE CARBOXYPEPTIDASE (E.C.3.4.16.4)

The largest off-origin peak in the Patterson function is 6.99% 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