scPDB - 2cig entry

Protein Data Bank Entry:

PDB ID : 2cig

Resolution :1.900 Å

Experimental Method : X-ray

Deposition Date : 2006-03-20

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_MYCTU
AC:	P9WNX1
Organism:	Mycobacterium tuberculosis
Reign:	Bacteria
TaxID:	83332
EC Number:	1.5.1.3

Chains:

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

Ligand binding site composition:

B-Factor:	19.849
Number of residues:	49
Including
Standard Amino Acids:	48
Non Standard Amino Acids:	0
Water Molecules:	1
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.261	1029.375

% Hydrophobic	% Polar
51.15	48.85
According to VolSite

Ligand :

HET Code:	1DG
Formula:	C27H29N8O18P3
Molecular weight:	846.483 g/mol
DrugBank ID:	-
Buried Surface Area:	69.02 %
Polar Surface area:	434.86 Å2

Number of
H-Bond Acceptors:	24
H-Bond Donors:	5
Rings:	6
Aromatic rings:	3
Anionic atoms:	4
Cationic atoms:	0
Rule of Five Violation:	2
Rotatable Bonds:	15

Mass center Coordinates

X	Y	Z
10.7613	-18.0223	-7.84229

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
OAC	N	ALA- 7	2.94	172.08	H-Bond (Protein Donor)	false
NAA	O	ALA- 7	2.87	144.99	H-Bond (Ligand Donor)	false
NAA	O	ILE- 14	2.98	154.09	H-Bond (Ligand Donor)	false
C1'	CG1	ILE- 20	4.49	0	Hydrophobic	false
CAU	CD1	ILE- 20	3.79	0	Hydrophobic	false
CBV	CB	ARG- 44	4.24	0	Hydrophobic	false
OBG	N	ARG- 44	3.29	140.23	H-Bond (Protein Donor)	false
OAK	NE	ARG- 44	2.68	160.34	H-Bond (Protein Donor)	false
OAL	NH2	ARG- 44	2.79	166.55	H-Bond (Protein Donor)	false
OAK	CZ	ARG- 44	3.57	0	Ionic (Protein Cationic)	false
OAL	CZ	ARG- 44	3.6	0	Ionic (Protein Cationic)	false
C5'	CB	ARG- 45	4.18	0	Hydrophobic	false
CAY	CG	ARG- 45	4.19	0	Hydrophobic	false
OAM	CZ	ARG- 45	3.76	0	Ionic (Protein Cationic)	false
OAM	NH1	ARG- 45	2.76	162.4	H-Bond (Protein Donor)	false
OBE	N	ARG- 45	3.32	151.72	H-Bond (Protein Donor)	false
C5'	CG2	VAL- 46	3.86	0	Hydrophobic	false
OAN	N	VAL- 46	2.91	130.62	H-Bond (Protein Donor)	false
C2'	CB	SER- 49	4.42	0	Hydrophobic	false
OAK	OG	SER- 66	2.78	162.76	H-Bond (Protein Donor)	false
OAE	N	ARG- 67	2.88	155.26	H-Bond (Protein Donor)	false
OAK	NE2	GLN- 68	2.91	137.17	H-Bond (Protein Donor)	false
OAG	N	GLY- 96	2.99	144.12	H-Bond (Protein Donor)	false
O5'	N	GLY- 97	3.27	144.41	H-Bond (Protein Donor)	false
OAF	N	GLN- 98	2.84	157.49	H-Bond (Protein Donor)	false
CAY	CB	GLN- 98	4.12	0	Hydrophobic	false
OAG	N	VAL- 99	3.29	145.15	H-Bond (Protein Donor)	false
CBT	CZ	TYR- 100	4.43	0	Hydrophobic	false
C4'	CB	ALA- 126	3.61	0	Hydrophobic	false