wwPDB validation report of PDB entry 3GCT

3GCT
THE GAMMA CHYMOTRYPSIN MOLECULE IS COMPRISED OF THREE
POLYPEPTIDE CHAINS WHICH ARE DERIVED FROM THE ZYMOGEN OF
THIS ENZYME BY EXCISION OF RESIDUES 14-15 AND 147-148. TO
ASSIGN SEPARATE CHAIN IDENTIFIERS TO THE THREE CHAINS
WOULD OBSCURE THIS RELATIONSHIP AND SO THIS WAS NOT DONE.
CHAIN TERMINATOR RECORDS WERE INSERTED AFTER RESIDUES 146
AND 245 TO INDICATE EXPLICIT TERMINI AND THE SPECIAL CODE
EXC WAS USED IN THE SEQRES RECORDS TO DENOTE THE EXCISIONS.
RESIDUES 11 THROUGH 13 AND 149 THROUGH 150 ARE NOT VISIBLE
IN THE ELECTRON DENSITY MAP AND SO ARE OMITTED. IN THE
ABSENCE OF RESIDUE 13 THE TER RECORD WHICH WOULD HAVE
APPEARED AFTER RESIDUE 13 IS ALSO OMITTED.

RESIDUES B 500 - B 504 ARE A TETRAPEPTIDE BOUND IN THE
ACTIVE SITE, COVALENTLY LINKED TO OG OF SER 195 AS AN ACYL
ADDUCT. IT IS, PRESUMABLY, AN AUTOLYTIC CLEAVAGE PRODUCT.
THE EXACT IDENTITY OF THE RESIDUES IS UNCERTAIN AS THE SIDE
CHAINS SEEM TO BE DISORDERED. THE ATOM IDENTIFIED AS
C UNK B 500 IS ACTUALLY THE CARBONYL CARBON OF AN
UNIDENTIFIED AMINO ACID NOT VISIBLE IN THE ELECTRON DENSITY
MAP.

STRUCTURE OF GAMMA-*CHYMOTRYPSIN IN THE RANGE $P*H 2.0 TO $P*H 10.5 SUGGESTS THAT GAMMA-CHYMOTRYPSIN IS A COVALENT ACYL-ENZYME ADDUCT AT LOW $P*H

RESIDUES WHICH FORM THE CATALYTIC CENTER OF THE MOLECULE

RESIDUES WHICH ARE INVOLVED IN THE SUBSTRATE BINDING SITE

BINDING SITE FOR CHAIN B OF UNK PRO GLY ALA TYR PEPTIDE

The largest off-origin peak in the Patterson function is 4.50% 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