5ZMP

The structure of a lysine deacylase


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.19 Å
  • R-Value Free: 0.215 
  • R-Value Work: 0.173 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

The structure of a lysine deacylase

Ge, F.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
lysine deacylase307Picosynechococcus sp. PCC 73109Mutation(s): 0 
Gene Names: SYNPCC7002_A2791
UniProt
Find proteins for B1XMP1 (Picosynechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6))
Explore B1XMP1 
Go to UniProtKB:  B1XMP1
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupB1XMP1
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ZN
Query on ZN

Download Ideal Coordinates CCD File 
B [auth A]ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.19 Å
  • R-Value Free: 0.215 
  • R-Value Work: 0.173 
  • Space Group: P 41
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 56.79α = 90
b = 56.79β = 90
c = 112.52γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
HKL-3000data reduction
HKL-3000data scaling
MOLREPphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

  • Released Date: 2019-02-06 
  • Deposition Author(s): Ge, F.

Revision History  (Full details and data files)

  • Version 1.0: 2019-02-06
    Type: Initial release
  • Version 1.1: 2023-11-22
    Changes: Data collection, Database references, Refinement description