wwPDB validation report of PDB entry 1W88

PYRUVATE DEHYDROGENASE E1 COMPONENT, ALPHA SUBUNIT

PYRUVATE DEHYDROGENASE E1 COMPONENT, BETA SUBUNIT

DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE
PERIPHERAL SUBUNIT BINDING DOMAIN (PSBD), RESIDUES 127-169

E2, DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX

DIHYDROLIPOYL TRANSACETYLASE CATALYTIC DOMAIN (RESIDUES 184-425) FROM BACILLUS STEAROTHERMOPHILUS

DIHYDROLIPOAMIDE DEHYDROGENASE COMPLEXED WITH THE BINDING DOMAIN OF THE DIHYDROLIPOAMIDE ACETYLASE

DIHYDROLIPOAMIDE ACETYLTRANSFERASE (E2P) SUBUNIT OF THE PYRUVATE DEHYDROGENASE (PDH) MULTIENZYME COMPLEX (LIPOYLATED DOMAIN, RESIDUES 1 - 80) (NMR, 11 STRUCTURES)

DIHYDROLIPOAMIDE ACETYLTRANSFERASE (E2P) SUBUNIT OF THE PYRUVATE DEHYDROGENASE (PDH) MULTIENZYME COMPLEX (LIPOYLATED DOMAIN, RESIDUES 1 - 80) (NMR, AVERAGE STRUCTURE)

NMR STRUCTURE OF THE PERIPHERAL-SUBUNIT BINDING DOMAIN OF BACILLUS STEAROTHERMOPHILUS E2P

PERIPHERAL-SUBUNIT BINDING DOMAINS FROM MESOPHILIC, THERMOPHILIC, AND HYPERTHERMOPHILIC BACTERIA FOLD BY ULTRAFAST, APPARENTLY TWO- STATE TRANSITIONS

PERIPHERAL-SUBUNIT FROM MESOPHILIC, THERMOPHILIC AND HYPERTHERMOPHILIC BACTERIA FOLD BY ULTRAFAST, APPARENTLY TWO-STATE TRANSITIONS

PERIPHERAL-SUBUNIT BINDING DOMAINS FROM MESOPHILIC, THERMOPHILIC, AND HYPERTHERMOPHILIC BACTERIA FOLD BY ULTRAFAST, APPARENTLY TWO- STATE FOLDING TRANSITIONS

THE CRYSTAL STRUCTURE OF PYRUVATE DEYDROGENASE E1 BOUND TO THE PERIPHERAL SUBUNIT BINDING DOMAIN OF E2

DIHYDROLIPOAMIDE ACETYLTRANSFERASE (E2P) SUBUNIT OF THE PYRUVATE DEHYDROGENASE (PDH) MULTIENZYME COMPLEX (PYRUVATE DECARBOXYLASE (E1P) / DIHYDROLIPOAMIDE DEHYDROGENASE (E3) 43 RESIDUE BINDING DOMAIN) (NMR, 35 STRUCTURES)

DIHYDROLIPOAMIDE ACETYLTRANSFERASE (E2P) SUBUNIT OF THE PYRUVATE DEHYDROGENASE (PDH) MULTIENZYME COMPLEX (PYRUVATE DECARBOXYLASE (E1P) / DIHYDROLIPOAMIDE DEHYDROGENASE (E3) 43 RESIDUE BINDING DOMAIN) (NMR, AVERAGE STRUCTURE)

ENGINEERED MUTATION ASP 180 ASN AND GLU 183 GLN IN CHAINS A, C, E AND G

THE FOLLOWING TERMINAL RESIDUES COULD NOT BE IDENTIFIED FROM THE ELECTRON DENSITY MAP AND ARE NOT MODELLED: A1-A4, A368, C1-C4, E1-E4, G1-G4, I122-I127, I168-I170, J122-J127, J170. IN ADDITION, THE FOLLOWING RESIDUES COULD NOT BE MODELLED: A269-A291, C269-C289, E206- E215, E266-E291, F81-F86, F120-F127, G206-G212, G266-G291, H122-H128. FURTHER, THE ELECTRON DENSITY FOR THE SECOND E1-E2 PSBD COMPLEX (CORRESPONDING TO CHAINS E, F, G, H AND J) IN THE ASYMMETRIC UNIT IS NOT AS WELL DEFINED AS THE FIRST (CORRESPONDING TO CHAINS A, B, C, D AND I)
The crystal structure of pyruvate dehydrogenase E1(D180N,E183Q) bound to the peripheral subunit binding domain of E2

FOR THE HETERO-ASSEMBLY DESCRIBED BY REMARK
350FOR THE HETERO-ASSEMBLY DESCRIBED BY REMARK
350

The largest off-origin peak in the Patterson function is 7.15% of the height of the origin peak. No significant pseudotranslation is detected.
structure factor analysis and validation
geometric validation package for ligand chemistry in protein x-ray structures
20191225.v01 (using entries in the PDB archive December 25th 2019)