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sc-PDB

An Annotated Database of Druggable Binding Sites from the Protein DataBank

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Protein Data Bank Entry:

2fz8

1.480 Å

X-ray

2006-02-09

Activity from ChEMBL: What is pChEMBL ?
MinMeanMedianStandard DeviationMaxCount
pChEMBL:7.7207.7207.7200.0007.7201

List of CHEMBLId :

CHEMBL10372


Interactomes:
Molecular Function:
Binding Site :

Uniprot Annotation

Name:Aldose reductase
ID:ALDR_HUMAN
AC:P15121
Organism:Homo sapiens
Reign:Eukaryota
TaxID:9606
EC Number:1.1.1.21


Chains:

Chain Name:Percentage of Residues
within binding site
A100 %


Ligand binding site composition:

B-Factor:11.642
Number of residues:33
Including
Standard Amino Acids: 32
Non Standard Amino Acids: 1
Water Molecules: 0
Cofactors: NAP
Metals:

Cavity properties

LigandabilityVolume (Å3)
1.098570.375

% Hydrophobic% Polar
63.3136.69
According to VolSite

Created with Highcharts 4.0.1Chart context menuDistribution of cavity propertiesscPDB Median2fz8HydrophobicAromaticHBond AcceptorHBond DonorHBondAcceptor/DonorPositive IonizableNegativeIonizableDummy80204060Highcharts.com
Ligand :
2fz8_1 Structure
HET Code: ZST
Formula: C19H11F3N3O3S
Molecular weight: 418.369 g/mol
DrugBank ID: DB08772
Buried Surface Area:78.83 %
Polar Surface area: 113.93 Å2
Number of
H-Bond Acceptors: 5
H-Bond Donors: 0
Rings: 4
Aromatic rings: 3
Anionic atoms: 1
Cationic atoms: 0
Rule of Five Violation: 0
Rotatable Bonds: 5

Mass center Coordinates

XYZ
16.4223-6.4473814.1629
Created with Highcharts 4.0.1Chart context menuDistribution of ligand propertiesscPDB Median2fz8RingsAromatic RingsHBond AcceptorHBond DonorRotatable BondsPositive IonizableNegativeIonizableRO5 Violation80510Highcharts.com


Binding mode :
What is Poseview ?
  • 2D View
  • 3D View
Binding mode
BioSolveIT Image generated by PoseView
Protein
Binding Site
Ligand
Interaction pattern
hydrophobic (CA)
aromatic (CZ)
hydrogen bond acceptor (O)
hydrogen bond acceptor/donor (OG)
hydrogen bond donor (N)
positively ionized (NZ)
negatively ionized (OD1)
metal (ZN)

Legend:

Represent the protein/ligand binding mode, centered on the ligand
Dashed lines represents hydrogen bonds and metal interactions
Green residue labels for amino acids with hydrophobic contacts (green lines) to the ligand

Image generated using PoseView by BioSolveIT
BioSolveIT


LigandProteinInteraction
AtomAtomResidueDistance
(Å)
Angle (°)Type
C17CD2TRP- 203.690Hydrophobic
C6CG2VAL- 474.410Hydrophobic
C7CG1VAL- 474.140Hydrophobic
C17CE1TYR- 484.260Hydrophobic
O3OHTYR- 482.74156.56H-Bond
(Protein Donor)
S1CH2TRP- 794.130Hydrophobic
C13SGCYS- 804.310Hydrophobic
O3NE2HIS- 1102.66152.32H-Bond
(Protein Donor)
S1CZ2TRP- 1113.760Hydrophobic
F1CD2TRP- 1113.890Hydrophobic
C14CBTRP- 1113.810Hydrophobic
C19CE3TRP- 1113.720Hydrophobic
O2NE1TRP- 1112.96162.1H-Bond
(Protein Donor)
DuArDuArTRP- 1113.380Aromatic Face/Face
F1CGPRO- 1124.450Hydrophobic
F2CG2THR- 1133.220Hydrophobic
S1CZPHE- 1223.770Hydrophobic
C9CH2TRP- 2193.450Hydrophobic
C9CBCYS- 2984.230Hydrophobic
C17SGCYS- 2984.170Hydrophobic
C9CBLEU- 3004.130Hydrophobic
C16CBLEU- 3004.450Hydrophobic
N3NLEU- 3003.21166.06H-Bond
(Protein Donor)
C14SGCYS- 3034.170Hydrophobic
C15CBCYS- 3033.990Hydrophobic
F2CBCYS- 3033.220Hydrophobic
F3CGTYR- 3094.050Hydrophobic
F2CD1TYR- 3093.560Hydrophobic
F1CGPRO- 3103.930Hydrophobic
F3CGPRO- 3103.780Hydrophobic
C17C4NNAP- 5003.530Hydrophobic