scPDB - 1jnr entry

Protein Data Bank Entry:

PDB ID : 1jnr

Resolution :1.600 Å

Experimental Method : X-ray

Deposition Date : 2001-07-25

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Adenylylsulfate reductase, subunit A (AprA)
ID:	O28603_ARCFU
AC:	O28603
Organism:	Archaeoglobus fulgidus
Reign:	Archaea
TaxID:	224325
EC Number:	/

Chains:

Chain Name:	Percentage of Residues within binding site
C	97 %
D	3 %

Ligand binding site composition:

B-Factor:	8.606
Number of residues:	82
Including
Standard Amino Acids:	74
Non Standard Amino Acids:	0
Water Molecules:	8
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.965	992.250

% Hydrophobic	% Polar
45.58	54.42
According to VolSite

Ligand :

HET Code:	FAD
Formula:	C27H31N9O15P2
Molecular weight:	783.534 g/mol
DrugBank ID:	DB03147
Buried Surface Area:	82.54 %
Polar Surface area:	381.7 Å2

Number of
H-Bond Acceptors:	22
H-Bond Donors:	7
Rings:	6
Aromatic rings:	3
Anionic atoms:	2
Cationic atoms:	0
Rule of Five Violation:	3
Rotatable Bonds:	13

Mass center Coordinates

X	Y	Z
42.7658	-0.613547	82.7518

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
O1A	N	PHE- 32	3.19	168.3	H-Bond (Protein Donor)	false
C4'	CB	PHE- 32	4.28	0	Hydrophobic	false
O2P	N	SER- 33	2.88	155.67	H-Bond (Protein Donor)	false
O2P	OG	SER- 33	2.62	164.29	H-Bond (Protein Donor)	false
C7M	CZ2	TRP- 48	4.34	0	Hydrophobic	false
C8M	CH2	TRP- 48	3.78	0	Hydrophobic	false
O3B	OE2	GLU- 56	2.68	160.48	H-Bond (Ligand Donor)	false
O3B	OE1	GLU- 56	3.23	125.4	H-Bond (Ligand Donor)	false
O2B	OE1	GLU- 56	2.59	155.88	H-Bond (Ligand Donor)	false
N3A	N	LYS- 57	3.14	139.82	H-Bond (Protein Donor)	false
C3B	CB	SER- 63	4.24	0	Hydrophobic	false
O3B	OG	SER- 63	2.79	140.46	H-Bond (Protein Donor)	false
O2A	N	ALA- 65	2.82	163.19	H-Bond (Protein Donor)	false
C2'	CB	ALA- 65	4.49	0	Hydrophobic	false
C8M	CB	ALA- 65	3.57	0	Hydrophobic	false
C6	CD2	LEU- 70	4.12	0	Hydrophobic	false
C9A	CD2	LEU- 70	3.94	0	Hydrophobic	false
C2'	CD1	LEU- 70	4.36	0	Hydrophobic	false
N3	O	ALA- 72	2.68	133.88	H-Bond (Ligand Donor)	false
O2	N	ASN- 74	2.91	179.14	H-Bond (Protein Donor)	false
N6A	O	ILE- 176	2.87	162.79	H-Bond (Ligand Donor)	false
N1A	N	ILE- 176	3.14	165.67	H-Bond (Protein Donor)	false
C7M	CE2	TRP- 234	3.92	0	Hydrophobic	false
C8M	CD1	TYR- 235	3.53	0	Hydrophobic	false
C8M	CB	ALA- 236	4.33	0	Hydrophobic	false
O2A	OD2	ASP- 239	2.61	176.33	H-Bond (Protein Donor)	false
N6A	OG	SER- 242	2.99	166.51	H-Bond (Ligand Donor)	false
C6	CE	MET- 365	3.5	0	Hydrophobic	false
C3'	CB	SER- 397	4.45	0	Hydrophobic	false
C5'	CB	SER- 397	4.04	0	Hydrophobic	false
O3'	OG	SER- 397	2.77	163.99	H-Bond (Ligand Donor)	false
O1P	N	ASP- 439	2.77	177.73	H-Bond (Protein Donor)	false
C1'	CD2	PHE- 448	4.37	0	Hydrophobic	false
N1	N	SER- 449	3.25	145.66	H-Bond (Protein Donor)	false
O2	OG	SER- 449	2.54	160.22	H-Bond (Protein Donor)	false
O2	N	SER- 449	3.11	151.99	H-Bond (Protein Donor)	false
C2'	CB	SER- 449	4.49	0	Hydrophobic	false
C5'	CB	SER- 452	4.1	0	Hydrophobic	false
O2P	O	HOH- 5008	2.6	166.9	H-Bond (Protein Donor)	false
O1A	O	HOH- 5048	2.88	179.96	H-Bond (Protein Donor)	false
O2B	O	HOH- 5059	2.89	179.98	H-Bond (Protein Donor)	false
N7A	O	HOH- 5197	2.89	157.05	H-Bond (Protein Donor)	false
O1P	O	HOH- 5320	2.68	172.12	H-Bond (Protein Donor)	false