3AKN

X-ray structure of iFABP from human and rat with bound fluorescent fatty acid analogue


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.257 
  • R-Value Work: 0.225 
  • R-Value Observed: 0.226 

Starting Model: experimental
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wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history


Literature

Crystal structures of human and rat intestinal fatty acid binding protein in complex with 11-(Dansylamino)undecanoic acid

Laguerre, A.J.K.Wielens, J.Parker, M.W.Porter, C.J.Scanlon, M.J.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Fatty acid-binding protein, intestinal131Rattus norvegicusMutation(s): 0 
Gene Names: Fabp2Fabpi
UniProt
Find proteins for P02693 (Rattus norvegicus)
Explore P02693 
Go to UniProtKB:  P02693
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP02693
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
11D
Query on 11D

Download Ideal Coordinates CCD File 
B [auth A]11-({[5-(dimethylamino)naphthalen-1-yl]sulfonyl}amino)undecanoic acid
C23 H34 N2 O4 S
CEPGVMDMVJGHFQ-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.257 
  • R-Value Work: 0.225 
  • R-Value Observed: 0.226 
  • Space Group: P 43 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 50.59α = 90
b = 50.59β = 90
c = 97.452γ = 90
Software Package:
Software NamePurpose
Blu-Icedata collection
AMoREphasing
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-07-20
    Type: Initial release
  • Version 1.1: 2023-11-01
    Changes: Data collection, Database references, Derived calculations, Refinement description