wwPDB validation report of PDB entry 2WS3

FAD ATOM C8M IS COVALENTLY LINKED TO NE2 OF SDHA HIS45
SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT

SUCCINATE DEHYDROGENASE IRON-SULFUR SUBUNIT

SUCCINATE DEHYDROGENASE CYTOCHROME B-556 SUBUNIT

SUCCINATE DEHYDROGENASE HYDROPHOBIC MEMBRANE ANCHOR SUBUNIT

CRYSTAL STRUCTURE OF THE E. COLI SUCCINATE: QUINONE OXIDOREDUCTASE (SQR) SDHB HIS207THR MUTANT

E. COLI SUCCINATE:QUINONE OXIDOREDUCTASE (SQR ) WITH CARBOXIN BOUND

E. COLI SUCCINATE:QUINONE OXIDOREDUCTASE (SQR ) WITH PENTACHLOROPHENOL BOUND

MOLECULAR ARCHITECTURE OF SUCCINATE DEHYDROGENASE (COMPLEXII) PREVENTS REACTIVE OXYGEN SPECIES GENERATION

CRYSTAL STRUCTURE OF THE E. COLI SUCCINATE: QUINONE OXIDOREDUCTASE (SQR) SDHC HIS84MET MUTANT

COMPLEX II (SUCCINATE DEHYDROGENASE) FROM E. COLI WITHATPENIN A5 INHIBITOR CO-CRYSTALLIZED AT THE UBIQUINONEBINDING SITE

CRYSTAL STRUCTURE OF THE E. COLI SUCCINATE: QUINONE OXIDOREDUCTASE (SQR) SDHD HIS71MET MUTANT

E. COLI SUCCINATE:QUINONE OXIDOREDUCTASE (SQR ) WITH AN EMPTY QUINONE-BINDING POCKET

ENGINEERED RESIDUE IN CHAIN D, TYR 83 TO PHE ENGINEERED RESIDUE IN CHAIN H, TYR 83 TO PHE ENGINEERED RESIDUE IN CHAIN L, TYR 83 TO PHE

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. DENSITY FOR THE N-TERMINUS OF SDH C (RESIDUES 1-7 OF CHAINS C, G, K) AND THE N-TERMINUS OF SDHD (RESIDUES 1-10 OF CHAINS D, H AND L) WAS WEAK AND THESE REGIONS ARE NOT INCLUDED IN THE MODEL. THE SIDE CHAIN OF SDHD TRP113 IS TRUNCATED AT THE CBETA ATOM SINCE DENSITY FOR THE SIDE CHAIN WAS POOR. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS.

SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT (E.C.1.3.99.1), SUCCINATE DEHYDROGENASE IRON-SULFUR SUBUNIT (E.C.1.3.99.1), SUCCINATE DEHYDROGENASE CYTOCHROME B-556 SUBUNIT (E.C.1.3.5.1), SUCCINATE DEHYDROGENASE HYDROPHOBIC MEMBRANE ANCHOR SUBUNIT (E.C.1.3.5.1)
Crystal structure of the E. coli succinate:quinone oxidoreductase (SQR) SdhD Tyr83Phe mutant

The largest off-origin peak in the Patterson function is 2.11% 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