9QYP | pdb_00009qyp

Crystal structure of leaf branch compost cutinase variant


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.01 Å
  • R-Value Free: 
    0.250 (Depositor), 0.250 (DCC) 
  • R-Value Work: 
    0.208 (Depositor), 0.208 (DCC) 

Starting Model: experimental
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wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history


Literature

Application of a Rational Crystal Contact Engineering Strategy on a Poly(ethylene terephthalate)-Degrading Cutinase

Walla, B.Dietrich, A.M.Brames, E.Bischoff, D.Fritzsche, S.Castiglione, K.Janowski, R.Niessing, D.Weuster-Botz, D.

(2025) Bioengineering 


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Leaf-branch compost cutinaseA [auth C],
B [auth A],
C [auth B]
267uncultured bacteriumMutation(s): 0 
EC: 3.1.1.74 (PDB Primary Data), 3.1.1.101 (PDB Primary Data)
UniProt
Find proteins for G9BY57 (Unknown prokaryotic organism)
Explore G9BY57 
Go to UniProtKB:  G9BY57
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupG9BY57
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.01 Å
  • R-Value Free:  0.250 (Depositor), 0.250 (DCC) 
  • R-Value Work:  0.208 (Depositor), 0.208 (DCC) 
Space Group: I 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 97.91α = 90
b = 101.87β = 90
c = 265.81γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
XDSdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
German Research Foundation (DFG)GermanyWE2715/14-2

Revision History  (Full details and data files)

  • Version 1.0: 2025-07-02
    Type: Initial release