9O2O | pdb_00009o2o

cis-CaaD E114Q mutant with a covalent hydroxypropionate intermediate of the hydration of acetylenecarboxylic acid


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.93 Å
  • R-Value Free: 
    0.238 (Depositor), 0.237 (DCC) 
  • R-Value Work: 
    0.214 (Depositor), 0.216 (DCC) 
  • R-Value Observed: 
    0.216 (Depositor) 

Starting Model: experimental
View more details

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.0 of the entry. See complete history


Literature

cis-CaaD E114Q mutant with a covalent hydroxypropionate intermediate of the hydration of acetylenecarboxylic acid

Silva, K.Geiger, J.H.Draths, K.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Cis-3-chloroacrylic acid dehalogenase
A, B, C
164coryneform bacteriumMutation(s): 1 
Gene Names: cis-caaD
UniProt
Find proteins for Q6VPE5 (coryneform bacterium)
Explore Q6VPE5 
Go to UniProtKB:  Q6VPE5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ6VPE5
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.93 Å
  • R-Value Free:  0.238 (Depositor), 0.237 (DCC) 
  • R-Value Work:  0.214 (Depositor), 0.216 (DCC) 
  • R-Value Observed: 0.216 (Depositor) 
Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 60.374α = 90
b = 100.42β = 90
c = 147.177γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Not funded--

Revision History  (Full details and data files)

  • Version 1.0: 2025-04-16
    Type: Initial release