scPDB - 1ai9 entry

Protein Data Bank Entry:

PDB ID : 1ai9

Resolution :1.850 Å

Experimental Method : X-ray

Deposition Date : 1997-05-01

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Dihydrofolate reductase
ID:	DYR_CANAX
AC:	P22906
Organism:	Candida albicans
Reign:	Eukaryota
TaxID:	5476
EC Number:	1.5.1.3

Chains:

Chain Name:	Percentage of Residues within binding site
B	100 %

Ligand binding site composition:

B-Factor:	16.357
Number of residues:	45
Including
Standard Amino Acids:	43
Non Standard Amino Acids:	0
Water Molecules:	2
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.504	901.125

% Hydrophobic	% Polar
60.67	39.33
According to VolSite

Ligand :

HET Code:	NDP
Formula:	C21H26N7O17P3
Molecular weight:	741.389 g/mol
DrugBank ID:	DB02338
Buried Surface Area:	71.05 %
Polar Surface area:	404.9 Å2

Number of
H-Bond Acceptors:	22
H-Bond Donors:	5
Rings:	5
Aromatic rings:	2
Anionic atoms:	4
Cationic atoms:	0
Rule of Five Violation:	2
Rotatable Bonds:	13

Mass center Coordinates

X	Y	Z
17.1015	32.6397	9.67277

Binding mode :

What is Poseview ?

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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
O7N	N	ALA- 11	2.97	153.83	H-Bond (Protein Donor)	false
N7N	O	ALA- 11	2.82	143.5	H-Bond (Ligand Donor)	false
N7N	O	ILE- 19	3.09	163.36	H-Bond (Ligand Donor)	false
O3D	O	LYS- 24	3.47	139.62	H-Bond (Ligand Donor)	false
C3N	CE	MET- 25	3.51	0	Hydrophobic	false
O1X	NH2	ARG- 56	3.34	145.14	H-Bond (Protein Donor)	false
O3X	NH2	ARG- 56	3.13	140.29	H-Bond (Protein Donor)	false
O1X	CZ	ARG- 56	3.69	0	Ionic (Protein Cationic)	false
O5B	N	LYS- 57	3.47	148.86	H-Bond (Protein Donor)	false
O3B	NZ	LYS- 57	2.96	166.25	H-Bond (Protein Donor)	false
C5B	CG	LYS- 57	4.06	0	Hydrophobic	false
O1A	N	THR- 58	3.09	125.01	H-Bond (Protein Donor)	false
O1A	OG1	THR- 58	2.58	167.1	H-Bond (Protein Donor)	false
C5N	CG2	THR- 58	4.37	0	Hydrophobic	false
O1X	OG	SER- 78	2.59	159.68	H-Bond (Protein Donor)	false
O2X	N	ARG- 79	3.02	152.58	H-Bond (Protein Donor)	false
O1A	N	GLY- 114	2.98	150.04	H-Bond (Protein Donor)	false
O2A	N	GLY- 114	3.14	122.2	H-Bond (Protein Donor)	false
O5D	N	ALA- 115	3.15	138.17	H-Bond (Protein Donor)	false
C5B	CB	GLU- 116	4.27	0	Hydrophobic	false
O2N	N	GLU- 116	3.08	160.4	H-Bond (Protein Donor)	false
N6A	OE2	GLU- 120	2.95	163.4	H-Bond (Ligand Donor)	false
C4D	CG2	THR- 147	3.95	0	Hydrophobic	false
N6A	O	HOH- 231	3.07	157.94	H-Bond (Ligand Donor)	false
O2N	O	HOH- 264	3.33	179.97	H-Bond (Protein Donor)	false