2Z6B

Crystal Structure Analysis of (gp27-gp5)3 conjugated with Fe(III) protoporphyrin

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.11 Å
  • R-Value Free: 0.315 
  • R-Value Work: 0.243 
  • R-Value Observed: 0.243 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history. 


Literature

Molecular design of heteroprotein assemblies providing a bionanocup as a chemical reactor.

Koshiyama, T., Yokoi, N., Ueno, T., Kanamaru, S., Nagano, S., Shiro, Y., Arisaka, F., Watanabe, Y.

(2008) Small 4: 50-54


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Tail-associated lysozyme584Tequatrovirus T4Mutation(s): 2 
Gene Names: 5
EC: 3.2.1.17
UniProt
Find proteins for P16009 (Enterobacteria phage T4)
Explore P16009 
Go to UniProtKB:  P16009
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP16009
Sequence Annotations
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  • Reference Sequence
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Baseplate structural protein Gp27B [auth D]391Tequatrovirus T4Mutation(s): 0 
Gene Names: 27
UniProt
Find proteins for P17172 (Enterobacteria phage T4)
Explore P17172 
Go to UniProtKB:  P17172
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP17172
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
NEN
Query on NEN
Download Ideal Coordinates CCD File 
C [auth A]1-ETHYL-PYRROLIDINE-2,5-DIONE
C6 H9 N O2
GHAZCVNUKKZTLG-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.11 Å
  • R-Value Free: 0.315 
  • R-Value Work: 0.243 
  • R-Value Observed: 0.243 
  • Space Group: H 3 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 138.536α = 90
b = 138.536β = 90
c = 389.121γ = 120
Software Package:
Software NamePurpose
CNSrefinement
HKL-2000data collection
HKL-2000data scaling
X-PLORphasing

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-04-15
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2021-11-10
    Changes: Database references, Derived calculations
  • Version 1.3: 2023-11-01
    Changes: Data collection, Refinement description