4IK2

G215S, A251G, T257A, D260G, T262D mutant of carboxypeptidase T from Thermoactinomyces vulgaris with N-BOC-L-Leu


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.40 Å
  • R-Value Free: 0.136 
  • R-Value Work: 0.125 
  • R-Value Observed: 0.125 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history


Literature

G215S, A251G, T257A, D260G, T262D mutant of carboxypeptidase T from Thermoactinomyces vulgaris with N-BOC-L-Leu

Timofeev, V.I.Kuznetsov, S.A.Akparov, V.K.Kuranova, I.P.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Carboxypeptidase T326Thermoactinomyces vulgarisMutation(s): 5 
Gene Names: cpt
EC: 3.4.17.18
UniProt
Find proteins for P29068 (Thermoactinomyces vulgaris)
Explore P29068 
Go to UniProtKB:  P29068
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP29068
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 4 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
BL2
Query on BL2

Download Ideal Coordinates CCD File 
D [auth A]N-(tert-butoxycarbonyl)-L-leucine
C11 H21 N O4
MDXGYYOJGPFFJL-QMMMGPOBSA-N
SO4
Query on SO4

Download Ideal Coordinates CCD File 
B [auth A]SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
ZN
Query on ZN

Download Ideal Coordinates CCD File 
C [auth A]ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
CA
Query on CA

Download Ideal Coordinates CCD File 
E [auth A],
F [auth A],
G [auth A],
H [auth A]
CALCIUM ION
Ca
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.40 Å
  • R-Value Free: 0.136 
  • R-Value Work: 0.125 
  • R-Value Observed: 0.125 
  • Space Group: P 63 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 158.243α = 90
b = 158.243β = 90
c = 104.657γ = 120
Software Package:
Software NamePurpose
HKL-2000data collection
PHASERphasing
REFMACrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-12-25
    Type: Initial release
  • Version 1.1: 2023-11-08
    Changes: Data collection, Database references, Derived calculations, Experimental preparation, Refinement description