5ZUM

Structure of dipeptidyl-peptidase III from Corallococcus sp. strain EGB

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.224 
  • R-Value Work: 0.174 
  • R-Value Observed: 0.176 

wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history. 


Literature

Structure of dipeptidyl peptidase III from Corallococcus sp. strain EGB

Zhang, H., Duan, Y.J., Li, Z.K., Liu, W.D., Huang, Y., Cui, Z.L.

To be published.

Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
dipeptidyl-peptidase III
A, B
537Corallococcus sp. EGBMutation(s): 0 
UniProt
Find proteins for A0A5H1ZR28 (Corallococcus sp. EGB)
Explore A0A5H1ZR28 
Go to UniProtKB:  A0A5H1ZR28
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A5H1ZR28
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A, B
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.224 
  • R-Value Work: 0.174 
  • R-Value Observed: 0.176 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 58.141α = 90
b = 77.85β = 90
c = 228.294γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
XSCALEdata scaling
PHENIXphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2019-06-12
    Type: Initial release