4PUU

Human Aldose Reductase complexed with a ligand with an IDD structure (2-(2-carbamoyl-5-fluoro-phenoxy)acetic acid) at 1.14 A


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.14 Å
  • R-Value Free: 0.156 
  • R-Value Work: 0.137 
  • R-Value Observed: 0.138 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history


Literature

Human Aldose Reductase: How expensive is the opening of the specificity pocket? IDD ligands under investigation

Rechlin, C.Heine, A.Scheer, F.Toth, P.Diederich, W.Klebe, G.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Aldose reductase316Homo sapiensMutation(s): 0 
Gene Names: AKR1B1ALDR1
EC: 1.1.1.21
UniProt & NIH Common Fund Data Resources
Find proteins for P15121 (Homo sapiens)
Explore P15121 
Go to UniProtKB:  P15121
PHAROS:  P15121
GTEx:  ENSG00000085662 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP15121
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
NAP
Query on NAP

Download Ideal Coordinates CCD File 
B [auth A]NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
C21 H28 N7 O17 P3
XJLXINKUBYWONI-NNYOXOHSSA-N
2WR
Query on 2WR

Download Ideal Coordinates CCD File 
C [auth A](2-carbamoyl-5-fluorophenoxy)acetic acid
C9 H8 F N O4
PCNZVPHJJYWUKQ-UHFFFAOYSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
2WR BindingDB:  4PUU -TΔS: min: -9.80e+0, max: 29.71 (kJ/mol) from 4 assay(s)
ΔH: min: -3.90e+1, max: -3.54e+1 (kJ/mol) from 2 assay(s)
ΔG: min: -3.89e+1, max: -2.94e+1 (kJ/mol) from 5 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.14 Å
  • R-Value Free: 0.156 
  • R-Value Work: 0.137 
  • R-Value Observed: 0.138 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 49.289α = 90
b = 66.394β = 91.82
c = 47.245γ = 90
Software Package:
Software NamePurpose
MAR345dtbdata collection
PHASERphasing
PHENIXrefinement
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: 2015-04-08
    Type: Initial release
  • Version 1.1: 2023-09-20
    Changes: Data collection, Database references, Derived calculations, Refinement description