scPDB - 2gq3 entry

Protein Data Bank Entry:

PDB ID : 2gq3

Resolution :2.300 Å

Experimental Method : X-ray

Deposition Date : 2006-04-19

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Malate synthase G
ID:	MASZ_MYCTU
AC:	P9WK17
Organism:	Mycobacterium tuberculosis
Reign:	Bacteria
TaxID:	83332
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	41.476
Number of residues:	45
Including
Standard Amino Acids:	44
Non Standard Amino Acids:	0
Water Molecules:	1
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.113	543.375

% Hydrophobic	% Polar
61.49	38.51
According to VolSite

Ligand :

HET Code:	COA
Formula:	C21H32N7O16P3S
Molecular weight:	763.502 g/mol
DrugBank ID:	DB01992
Buried Surface Area:	60.55 %
Polar Surface area:	426.11 Å2

Number of
H-Bond Acceptors:	21
H-Bond Donors:	6
Rings:	3
Aromatic rings:	2
Anionic atoms:	4
Cationic atoms:	0
Rule of Five Violation:	3
Rotatable Bonds:	18

Mass center Coordinates

X	Y	Z
46.7769	21.2773	81.247

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
N6A	O	VAL- 118	3.19	128.17	H-Bond (Ligand Donor)	false
O7A	CZ	ARG- 125	3.68	0	Ionic (Protein Cationic)	false
O9A	CZ	ARG- 125	4	0	Ionic (Protein Cationic)	false
O7A	NE	ARG- 125	2.78	172.92	H-Bond (Protein Donor)	false
O9A	NH1	ARG- 125	3.21	158.32	H-Bond (Protein Donor)	false
C5B	CZ	PHE- 126	3.79	0	Hydrophobic	false
CAP	CE1	PHE- 126	4.41	0	Hydrophobic	false
C2B	CE2	PHE- 126	3.45	0	Hydrophobic	false
N3A	ND2	ASN- 129	3.26	142.58	H-Bond (Protein Donor)	false
O8A	NZ	LYS- 305	3.28	164.24	H-Bond (Protein Donor)	false
O9A	NZ	LYS- 305	2.68	125.14	H-Bond (Protein Donor)	false
O8A	NZ	LYS- 305	3.28	0	Ionic (Protein Cationic)	false
O9A	NZ	LYS- 305	2.68	0	Ionic (Protein Cationic)	false
O7A	CZ	ARG- 312	3.32	0	Ionic (Protein Cationic)	false
O8A	CZ	ARG- 312	3.45	0	Ionic (Protein Cationic)	false
O8A	NH1	ARG- 312	2.73	161.11	H-Bond (Protein Donor)	false
O8A	NH2	ARG- 312	3.35	128.78	H-Bond (Protein Donor)	false
C2P	CG	MET- 515	4	0	Hydrophobic	false
S1P	CG2	THR- 517	4.15	0	Hydrophobic	false
CEP	CG2	THR- 519	4.22	0	Hydrophobic	false
N6A	O	PRO- 543	3.18	123.54	H-Bond (Ligand Donor)	false
C6P	SG	CYS- 619	3.59	0	Hydrophobic	false
CDP	SG	CYS- 619	4.01	0	Hydrophobic	false
O1A	NZ	LYS- 621	2.8	124.2	H-Bond (Protein Donor)	false
O1A	NZ	LYS- 621	2.8	0	Ionic (Protein Cationic)	false
CCP	CD	LYS- 621	4.41	0	Hydrophobic	false
CEP	CB	LYS- 621	4.3	0	Hydrophobic	false
CEP	CG	MET- 631	3.61	0	Hydrophobic	false
C6P	CG	MET- 631	3.98	0	Hydrophobic	false
C2P	CG	MET- 631	3.56	0	Hydrophobic	false
S1P	CB	MET- 631	3.42	0	Hydrophobic	false
CAP	CE	MET- 631	3.26	0	Hydrophobic	false
S1P	CB	ASP- 633	4.18	0	Hydrophobic	false