Logo scPDB

sc-PDB

An Annotated Database of Druggable Binding Sites from the Protein DataBank

Logo CNRS Logo Unistra
Protein Data Bank Entry:

2acs

1.760 Å

X-ray

1994-04-15

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:9.065
Number of residues:47
Including
Standard Amino Acids: 45
Non Standard Amino Acids: 0
Water Molecules: 2
Cofactors:
Metals:

Cavity properties

LigandabilityVolume (Å3)
0.742816.750

% Hydrophobic% Polar
49.5950.41
According to VolSite

Ligand :
2acs_1 Structure
HET Code: NAP
Formula: C21H25N7O17P3
Molecular weight: 740.381 g/mol
DrugBank ID: DB03461
Buried Surface Area:78.55 %
Polar Surface area: 405.54 Å2
Number of
H-Bond Acceptors: 21
H-Bond Donors: 5
Rings: 5
Aromatic rings: 3
Anionic atoms: 4
Cationic atoms: 1
Rule of Five Violation: 2
Rotatable Bonds: 13

Mass center Coordinates

XYZ
22.151526.925672.9159


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
O2DNTHR- 193.32146.85H-Bond
(Protein Donor)
O3DNTRP- 202.94144.92H-Bond
(Protein Donor)
C3DCBTRP- 203.740Hydrophobic
O1NNZLYS- 212.84149.44H-Bond
(Protein Donor)
O1NNZLYS- 212.840Ionic
(Protein Cationic)
O2DOD2ASP- 432.74150.78H-Bond
(Ligand Donor)
C2DCZTYR- 484.130Hydrophobic
N7NOGSER- 1592.89140.85H-Bond
(Ligand Donor)
O7NND2ASN- 1603.1164.03H-Bond
(Protein Donor)
N7NOE1GLN- 1833.04158.07H-Bond
(Ligand Donor)
C3NCBTYR- 2094.30Hydrophobic
DuArDuArTYR- 2093.550Aromatic Face/Face
O2NOGSER- 2102.7152.01H-Bond
(Protein Donor)
O5DNSER- 2103.12133.77H-Bond
(Protein Donor)
O1ANLEU- 2123.11142.4H-Bond
(Protein Donor)
C1BCD1LEU- 2124.290Hydrophobic
O1ANSER- 2143.06142.97H-Bond
(Protein Donor)
O2NOGSER- 2142.8150.34H-Bond
(Protein Donor)
C4BCGPRO- 2153.580Hydrophobic
C1BCGPRO- 2154.170Hydrophobic
C3BCBASP- 2164.270Hydrophobic
C4DCG1ILE- 2604.190Hydrophobic
O2ANLYS- 2622.88172.32H-Bond
(Protein Donor)
O1XNZLYS- 2622.79172.94H-Bond
(Protein Donor)
C5BCDLYS- 2623.880Hydrophobic
C3BCDLYS- 2623.920Hydrophobic
C5DCBLYS- 2623.930Hydrophobic
O1XNZLYS- 2622.790Ionic
(Protein Cationic)
O3XOGSER- 2632.8167.82H-Bond
(Protein Donor)
O1XNVAL- 2643.07155.22H-Bond
(Protein Donor)
O3XOG1THR- 2652.82158.31H-Bond
(Protein Donor)
O3XCZARG- 2683.850Ionic
(Protein Cationic)
N6AOE2GLU- 2713.07167.03H-Bond
(Ligand Donor)
N7AND2ASN- 2723.06170.99H-Bond
(Protein Donor)
N6AOD1ASN- 2722.89144.83H-Bond
(Ligand Donor)
C4NSGCYS- 2984.140Hydrophobic
N1AOHOH- 9172.93179.94H-Bond
(Protein Donor)