6VE6

A structural characterization of poly(aspartic acid) hydrolase-1 from Sphingomonas sp. KT-1.


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.45 Å
  • R-Value Free: 0.290 
  • R-Value Work: 0.236 
  • R-Value Observed: 0.238 

wwPDB Validation   3D Report Full Report

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This is version 1.1 of the entry. See complete history


Literature

Structural Characterization of Sphingomonas sp. KT-1 PahZ1-Catalyzed Biodegradation of Thermally Synthesized Poly(aspartic acid)

Brambley, C.A.Bolay, A.L.Salvo, H.Jansch, A.L.Yared, T.J.Miller, J.M.Wallen, J.R.Weiland, M.H.

(2020) ACS Sustain Chem Eng 


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Poly(Aspartic acid) hydrolase-1
A, B, C, D
295Sphingomonas sp. KT-1Mutation(s): 0 
Gene Names: pahZ
UniProt
Find proteins for Q7WSC1 (Sphingomonas sp. KT-1)
Explore Q7WSC1 
Go to UniProtKB:  Q7WSC1
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ7WSC1
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.45 Å
  • R-Value Free: 0.290 
  • R-Value Work: 0.236 
  • R-Value Observed: 0.238 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 81.749α = 90
b = 87.006β = 90
c = 171.06γ = 90
Software Package:
Software NamePurpose
HKL-3000data scaling
PHASERphasing
PHENIXrefinement
PDB_EXTRACTdata extraction
HKL-3000data reduction

Structure Validation

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Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Science Foundation (NSF, United States)United StatesDUE 1611988

Revision History  (Full details and data files)

  • Version 1.0: 2020-12-09
    Type: Initial release
  • Version 1.1: 2023-10-11
    Changes: Data collection, Database references, Refinement description