scPDB - 4gca entry

Protein Data Bank Entry:

PDB ID : 4gca

Resolution :0.900 Å

Experimental Method : X-ray

Deposition Date : 2012-07-30

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

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
A	100 %

Ligand binding site composition:

B-Factor:	7.980
Number of residues:	34
Including
Standard Amino Acids:	32
Non Standard Amino Acids:	1
Water Molecules:	1
Cofactors:	NAP
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.192	378.000

% Hydrophobic	% Polar
69.64	30.36
According to VolSite

Ligand :

HET Code:	2X9
Formula:	C17H12F3N2O2S
Molecular weight:	365.350 g/mol
DrugBank ID:	-
Buried Surface Area:	81.13 %
Polar Surface area:	94.15 Å2

Number of
H-Bond Acceptors:	4
H-Bond Donors:	0
Rings:	3
Aromatic rings:	3
Anionic atoms:	1
Cationic atoms:	0
Rule of Five Violation:	0
Rotatable Bonds:	4

Mass center Coordinates

X	Y	Z
-9.55336	2.85252	5.69768

Binding mode :

What is Poseview ?

2D View
3D View

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

Ligand	Protein		Interaction
Atom	Atom	Residue	Distance (Å)	Angle (°)	Type
C1	CE2	TRP- 20	3.77	0	Hydrophobic	false
C9	CE2	TRP- 20	3.52	0	Hydrophobic	false
C1	CG1	VAL- 47	4.23	0	Hydrophobic	false
C1	CE1	TYR- 48	4.42	0	Hydrophobic	false
C9	CE1	TYR- 48	3.98	0	Hydrophobic	false
O24	OH	TYR- 48	2.65	160.65	H-Bond (Protein Donor)	false
S30	CH2	TRP- 79	4.2	0	Hydrophobic	false
F38	CH2	TRP- 79	3.43	0	Hydrophobic	false
F38	SG	CYS- 80	3.39	0	Hydrophobic	false
O24	NE2	HIS- 110	2.66	148.32	H-Bond (Protein Donor)	false
F4	CE3	TRP- 111	3.94	0	Hydrophobic	false
C12	CZ2	TRP- 111	4.38	0	Hydrophobic	false
F13	CZ3	TRP- 111	3.66	0	Hydrophobic	false
S30	CZ2	TRP- 111	3.58	0	Hydrophobic	false
F38	CD2	TRP- 111	3.75	0	Hydrophobic	false
C37	CB	TRP- 111	4.07	0	Hydrophobic	false
O23	NE1	TRP- 111	2.88	165.2	H-Bond (Protein Donor)	false
DuAr	DuAr	TRP- 111	3.47	0	Aromatic Face/Face	false
F4	CG2	THR- 113	3.79	0	Hydrophobic	false
C37	CB	THR- 113	4.41	0	Hydrophobic	false
F38	CZ	PHE- 115	3.38	0	Hydrophobic	false
C11	CZ	PHE- 122	3.63	0	Hydrophobic	false
S30	CE1	PHE- 122	3.76	0	Hydrophobic	false
F38	CE1	PHE- 122	4.04	0	Hydrophobic	false
C11	CZ3	TRP- 219	3.68	0	Hydrophobic	false
C12	CH2	TRP- 219	3.52	0	Hydrophobic	false
C6	SG	CYS- 298	3.95	0	Hydrophobic	false
C12	SG	CYS- 298	4.39	0	Hydrophobic	false
F13	CB	ALA- 299	3.91	0	Hydrophobic	false
C11	CD2	LEU- 300	4.02	0	Hydrophobic	false
C12	CB	LEU- 300	4.34	0	Hydrophobic	false
C32	CB	LEU- 300	4.46	0	Hydrophobic	false
C36	CB	LEU- 300	4.22	0	Hydrophobic	false
F4	CB	CYS- 303	3.47	0	Hydrophobic	false
C36	CB	CYS- 303	4.06	0	Hydrophobic	false
C37	SG	CYS- 303	3.83	0	Hydrophobic	false
F4	CD1	TYR- 309	3.36	0	Hydrophobic	false
F13	CE1	TYR- 309	3.39	0	Hydrophobic	false
F13	CE2	PHE- 311	4.28	0	Hydrophobic	false
C9	C4N	NAP- 401	3.83	0	Hydrophobic	false