2IIH

Crystal structure of the molybdenum cofactor biosynthesis protein C (TTHA1789) from thermus theromophilus HB8 (H32 form)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.75 Å
  • R-Value Free: 0.217 
  • R-Value Work: 0.196 
  • R-Value Observed: 0.196 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Crystal structure of the molybdenum cofactor biosynthesis protein C (TTHA1789) from thermus theromophilus HB8 (H32 form)

Jeyakanthan, J.Kanaujia, S.P.Vasuki Ranjani, C.Sekar, K.Baba, S.Chen, L.Liu, Z.-J.Wang, B.-C.Ebihara, A.Kuramitsu, S.Shinkai, A.Shiro, Y.Yokoyama, S.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Molybdenum cofactor biosynthesis protein C157Thermus thermophilus HB8Mutation(s): 0 
UniProt
Find proteins for Q5SHE1 (Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8))
Explore Q5SHE1 
Go to UniProtKB:  Q5SHE1
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ5SHE1
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
PO4
Query on PO4

Download Ideal Coordinates CCD File 
B [auth A]PHOSPHATE ION
O4 P
NBIIXXVUZAFLBC-UHFFFAOYSA-K
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.75 Å
  • R-Value Free: 0.217 
  • R-Value Work: 0.196 
  • R-Value Observed: 0.196 
  • Space Group: H 3 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 106.573α = 90
b = 106.573β = 90
c = 59.251γ = 120
Software Package:
Software NamePurpose
CNSrefinement
HKL-2000data collection
HKL-2000data reduction
SCALEPACKdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2007-10-09
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Derived calculations, Source and taxonomy, Version format compliance
  • Version 1.2: 2023-10-25
    Changes: Data collection, Database references, Derived calculations, Refinement description