2EQ9

Crystal structure of lipoamide dehydrogenase from thermus thermophilus HB8 with psbdb


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.09 Å
  • R-Value Free: 0.257 
  • R-Value Work: 0.217 
  • R-Value Observed: 0.217 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

Crystal structure of lipoamide dehydrogenase from Thermus thermophilus HB8

Nakai, T.Kamiya, N.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Pyruvate dehydrogenase complex, dihydrolipoamide dehydrogenase E3 component
A, B, D, E, G
A, B, D, E, G, H, J, K
464Thermus thermophilus HB8Mutation(s): 0 
Gene Names: TTHA0233
EC: 1.8.1.4
UniProt
Find proteins for Q5SLR0 (Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8))
Explore Q5SLR0 
Go to UniProtKB:  Q5SLR0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ5SLR0
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Pyruvate dehydrogenase complex, dihydrolipoamide acetyltransferase E2 component
C, F, I, L
41Thermus thermophilus HB8Mutation(s): 0 
Gene Names: TTHA0232
EC: 2.3.1.168
UniProt
Find proteins for Q5SLR1 (Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8))
Explore Q5SLR1 
Go to UniProtKB:  Q5SLR1
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ5SLR1
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.09 Å
  • R-Value Free: 0.257 
  • R-Value Work: 0.217 
  • R-Value Observed: 0.217 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 88.781α = 89.26
b = 88.877β = 87.01
c = 144.149γ = 70.84
Software Package:
Software NamePurpose
CNSrefinement
HKL-2000data collection
HKL-2000data reduction
HKL-2000data scaling
AMoREphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-04-01
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Source and taxonomy, Version format compliance
  • Version 1.2: 2023-10-25
    Changes: Data collection, Database references, Derived calculations, Refinement description