scPDB - 1w29 entry

Protein Data Bank Entry:

PDB ID : 1w29

Resolution :2.300 Å

Experimental Method : X-ray

Deposition Date : 2004-07-01

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	6,7-dimethyl-8-ribityllumazine synthase
ID:	RISB_MYCTU
AC:	P9WHE9
Organism:	Mycobacterium tuberculosis
Reign:	Bacteria
TaxID:	83332
EC Number:	2.5.1.78

Chains:

Chain Name:	Percentage of Residues within binding site
B	62 %
C	38 %

Ligand binding site composition:

B-Factor:	12.725
Number of residues:	41
Including
Standard Amino Acids:	39
Non Standard Amino Acids:	0
Water Molecules:	2
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.242	573.750

% Hydrophobic	% Polar
43.53	56.47
According to VolSite

Ligand :

HET Code:	TS1
Formula:	C14H21N4O11P
Molecular weight:	452.310 g/mol
DrugBank ID:	DB02135
Buried Surface Area:	69.26 %
Polar Surface area:	244.89 Å2

Number of
H-Bond Acceptors:	11
H-Bond Donors:	6
Rings:	2
Aromatic rings:	0
Anionic atoms:	2
Cationic atoms:	0
Rule of Five Violation:	2
Rotatable Bonds:	11

Mass center Coordinates

X	Y	Z
-11.4752	17.9966	12.5072

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
C10	CE2	TRP- 27	4	0	Hydrophobic	false
C15	CZ3	TRP- 27	3.64	0	Hydrophobic	false
O2	N	ALA- 59	3.01	138.73	H-Bond (Protein Donor)	false
O19	N	ILE- 60	3.23	167.8	H-Bond (Protein Donor)	false
C12	CB	ILE- 60	4.04	0	Hydrophobic	false
O26	OE2	GLU- 61	2.91	172.62	H-Bond (Ligand Donor)	false
O21	OE1	GLU- 61	2.87	157.81	H-Bond (Ligand Donor)	false
O21	OE2	GLU- 61	3.4	143	H-Bond (Ligand Donor)	false
N3	O	VAL- 81	2.65	175.74	H-Bond (Ligand Donor)	false
C16	CG1	VAL- 82	4.39	0	Hydrophobic	false
O4	N	ILE- 83	3.17	149.32	H-Bond (Protein Donor)	false
O32	N	GLN- 86	2.94	148.55	H-Bond (Protein Donor)	false
O33	N	THR- 87	3.11	143.81	H-Bond (Protein Donor)	false
C14	CB	ALA- 113	4.26	0	Hydrophobic	false
O26	N	ASN- 114	2.65	159.6	H-Bond (Protein Donor)	false
O23	O	ASN- 114	3.13	151.65	H-Bond (Ligand Donor)	false
O31	NE	ARG- 128	2.56	166.62	H-Bond (Protein Donor)	false
O31	NH2	ARG- 128	3.48	123.41	H-Bond (Protein Donor)	false
O32	NH2	ARG- 128	3.2	178.03	H-Bond (Protein Donor)	false
O31	CZ	ARG- 128	3.45	0	Ionic (Protein Cationic)	false
O6	NZ	LYS- 138	3.04	138.46	H-Bond (Protein Donor)	false
C14	CB	ALA- 142	4.42	0	Hydrophobic	false
C14	CB	ALA- 145	4.2	0	Hydrophobic	false
O2	O	HOH- 2010	2.76	160.45	H-Bond (Protein Donor)	false