1ABE

NOVEL STEREOSPECIFICITY OF THE L-ARABINOSE-BINDING PROTEIN

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Observed: 0.137 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history. 



Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
L-ARABINOSE-BINDING PROTEIN306Escherichia coliMutation(s): 0 
UniProt
Find proteins for P02924 (Escherichia coli (strain K12))
Explore P02924 
Go to UniProtKB:  P02924
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP02924
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ARB
Query on ARB
Download Ideal Coordinates CCD File 
C [auth A]beta-L-arabinopyranose
C5 H10 O5
SRBFZHDQGSBBOR-KLVWXMOXSA-N
ARA
Query on ARA
Download Ideal Coordinates CCD File 
B [auth A]alpha-L-arabinopyranose
C5 H10 O5
SRBFZHDQGSBBOR-QMKXCQHVSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Observed: 0.137 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 55.46α = 90
b = 71.82β = 90
c = 77.84γ = 90
Software Package:
Software NamePurpose
PROLSQrefinement

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: 1993-10-31
    Type: Initial release
  • Version 1.1: 2008-03-10
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Data collection, Derived calculations, Other, Structure summary
  • Version 1.4: 2024-02-07
    Changes: Data collection, Database references, Structure summary