scPDB - 1wur entry

Protein Data Bank Entry:

PDB ID : 1wur

Resolution :1.820 Å

Experimental Method : X-ray

Deposition Date : 2004-12-08

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	GTP cyclohydrolase 1
ID:	Q5SH52_THET8
AC:	Q5SH52
Organism:	Thermus thermophilus
Reign:	Bacteria
TaxID:	300852
EC Number:	/

Chains:

Chain Name:	Percentage of Residues within binding site
C	52 %
D	48 %

Ligand binding site composition:

B-Factor:	28.544
Number of residues:	36
Including
Standard Amino Acids:	32
Non Standard Amino Acids:	1
Water Molecules:	3
Cofactors:
Metals:	ZN

Cavity properties

Ligandability	Volume (Å3)
0.200	330.750

% Hydrophobic	% Polar
48.98	51.02
According to VolSite

Ligand :

HET Code:	8DG
Formula:	C10H12N5O14P3
Molecular weight:	519.149 g/mol
DrugBank ID:	-
Buried Surface Area:	62.91 %
Polar Surface area:	329.85 Å2

Number of
H-Bond Acceptors:	16
H-Bond Donors:	4
Rings:	3
Aromatic rings:	0
Anionic atoms:	4
Cationic atoms:	0
Rule of Five Violation:	2
Rotatable Bonds:	8

Mass center Coordinates

X	Y	Z
5.8225	31.195	13.4223

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
C4'	CB	ALA- 87	4.13	0	Hydrophobic	false
C1'	CE2	PHE- 89	4.49	0	Hydrophobic	false
C4'	CZ	PHE- 89	4.05	0	Hydrophobic	false
C5'	CB	HIS- 110	4.36	0	Hydrophobic	false
O1B	NE2	HIS- 111	2.53	164.75	H-Bond (Protein Donor)	false
N2	O	LEU- 130	3.14	159.07	H-Bond (Ligand Donor)	false
O1G	OG	SER- 133	2.7	153.23	H-Bond (Protein Donor)	false
O3'	OG	SER- 133	2.51	158.74	H-Bond (Ligand Donor)	false
C2'	CB	SER- 133	4.06	0	Hydrophobic	false
O1G	NZ	LYS- 134	2.93	161.4	H-Bond (Protein Donor)	false
O3B	NZ	LYS- 134	3.26	125.58	H-Bond (Protein Donor)	false
O2A	NZ	LYS- 134	3.21	143.15	H-Bond (Protein Donor)	false
O1G	NZ	LYS- 134	2.93	0	Ionic (Protein Cationic)	false
O2A	NZ	LYS- 134	3.21	0	Ionic (Protein Cationic)	false
O1G	NE	ARG- 137	2.82	165.27	H-Bond (Protein Donor)	false
O1G	NH2	ARG- 137	3.25	135.72	H-Bond (Protein Donor)	false
O3G	NH2	ARG- 137	2.89	149.62	H-Bond (Protein Donor)	false
O1G	CZ	ARG- 137	3.47	0	Ionic (Protein Cationic)	false
O3G	CZ	ARG- 137	3.9	0	Ionic (Protein Cationic)	false
O6	N	GLN- 149	2.74	166.14	H-Bond (Protein Donor)	false
N1	OE1	GLU- 150	2.86	170.41	H-Bond (Protein Donor)	false
N2	OE2	GLU- 150	2.64	148.97	H-Bond (Ligand Donor)	false
N2	OE1	GLU- 150	3.19	141.55	H-Bond (Ligand Donor)	false
O2G	NH1	ARG- 183	2.85	176.63	H-Bond (Protein Donor)	false
O3G	NH2	ARG- 183	2.75	161.93	H-Bond (Protein Donor)	false
O2G	CZ	ARG- 183	3.68	0	Ionic (Protein Cationic)	false
O3G	CZ	ARG- 183	3.66	0	Ionic (Protein Cationic)	false
O1B	CZ	ARG- 183	3.77	0	Ionic (Protein Cationic)	false
O8	ZN	ZN- 1003	2.02	0	Metal Acceptor	false
O2G	O	HOH- 1008	2.97	156.42	H-Bond (Protein Donor)	false