4ZU6

Crystal Structure of O-Acetylserine Sulfhydrylase from Haemophilus influenzae in complex with pre-reactive o-acetyl serine, alpha-aminoacrylate reaction intermediate and Peptide inhibitor at the resolution of 2.25A


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.03 Å
  • R-Value Free: 0.230 
  • R-Value Work: 0.189 
  • R-Value Observed: 0.191 

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Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history


Literature

Crystal Structure of O-Acetylserine Sulfhydrylase from Haemophilus inuen-zae in complex with pre-reactive o-acetyl serine and peptide inhibitor

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

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Cysteine synthaseA [auth X]332Haemophilus influenzae Rd KW20Mutation(s): 0 
Gene Names: cysKHI_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

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
C-terminal peptide from Serine acetyltransferase10Salmonella enterica subsp. enterica serovar Typhimurium str. LT2Mutation(s): 0 
UniProt
Find proteins for P29847 (Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720))
Explore P29847 
Go to UniProtKB:  P29847
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP29847
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
PLP
Query on PLP

Download Ideal Coordinates CCD File 
D [auth X]PYRIDOXAL-5'-PHOSPHATE
C8 H10 N O6 P
NGVDGCNFYWLIFO-UHFFFAOYSA-N
OAS
Query on OAS

Download Ideal Coordinates CCD File 
C [auth X]O-ACETYLSERINE
C5 H9 N O4
VZXPDPZARILFQX-BYPYZUCNSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.03 Å
  • R-Value Free: 0.230 
  • R-Value Work: 0.189 
  • R-Value Observed: 0.191 
  • Space Group: I 41
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 112.634α = 90
b = 112.634β = 90
c = 43.49γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-06-10
    Type: Initial release
  • Version 1.1: 2023-11-08
    Changes: Data collection, Database references, Derived calculations, Refinement description, Source and taxonomy