4NU8

Crystal structure of O-acetylserine sulfhydrylase from Haemophilus influenzae in complex with high affinity inhibitory peptide from serine acetyl transferase of Salmonella typhimurium at 2.0 A

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.07 Å
  • R-Value Free: 0.235 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.189 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history. 


Literature

Crystal structure of O-acetylserine sulfhydrylase from Haemophilus influenzae in complex with high affinity inhibitory peptide from serine acetyl transferase of Salmonella Typhimurium at 2.0 A

Ekka, M.K., Kaushik, A., Singh, A.K., Kumaran, S.

To be published.

Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Cysteine synthaseA [auth X]322Haemophilus influenzae Rd KW20Mutation(s): 0 
Gene Names: cysK, HI_1103
EC: 2.5.1.47
UniProt
Find proteins for P45040 (Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd))
Explore P45040 
Go to UniProtKB:  P45040
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP45040
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Peptide from Serine acetyltransferaseB [auth A]8Salmonella enterica subsp. enterica serovar TyphiMutation(s): 0 
UniProt
Find proteins for P29847 (Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720))
Explore P29847 
Go to UniProtKB:  P29847
Entity Groups  
UniProt GroupP29847
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
GOL
Query on GOL
Download Ideal Coordinates CCD File 
C [auth X]GLYCEROL
C3 H8 O3
PEDCQBHIVMGVHV-UHFFFAOYSA-N
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
LLP
Query on LLP		A [auth X]L-PEPTIDE LINKINGC14 H22 N3 O7 PLYS
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.07 Å
  • R-Value Free: 0.235 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.189 
  • Space Group: I 41
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 112.322α = 90
b = 112.322β = 90
c = 45.8γ = 90
Software Package:
Software NamePurpose
HKL-2000data collection
PHASESphasing
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-12-03
    Type: Initial release
  • Version 1.1: 2023-11-08
    Changes: Data collection, Database references, Derived calculations, Refinement description
  • Version 1.2: 2023-12-06
    Changes: Data collection