scPDB - 1i0s entry

Protein Data Bank Entry:

PDB ID : 1i0s

Resolution :1.650 Å

Experimental Method : X-ray

Deposition Date : 2001-01-29

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Ferric-chelate reductase (NAD(P)H)
ID:	FERCR_ARCFU
AC:	O29428
Organism:	Archaeoglobus fulgidus
Reign:	Archaea
TaxID:	224325
EC Number:	/

Chains:

Chain Name:	Percentage of Residues within binding site
A	95 %
B	5 %

Ligand binding site composition:

B-Factor:	13.133
Number of residues:	41
Including
Standard Amino Acids:	36
Non Standard Amino Acids:	1
Water Molecules:	4
Cofactors:	NAP
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.459	378.000

% Hydrophobic	% Polar
33.93	66.07
According to VolSite

Ligand :

HET Code:	FMN
Formula:	C17H19N4O9P
Molecular weight:	454.328 g/mol
DrugBank ID:	DB03247
Buried Surface Area:	84.19 %
Polar Surface area:	217.05 Å2

Number of
H-Bond Acceptors:	12
H-Bond Donors:	4
Rings:	3
Aromatic rings:	1
Anionic atoms:	2
Cationic atoms:	0
Rule of Five Violation:	1
Rotatable Bonds:	7

Mass center Coordinates

X	Y	Z
25.2173	-10.1916	74.0321

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
C7M	CD1	LEU- 13	3.67	0	Hydrophobic	false
N1	NE2	GLN- 27	3.11	127.12	H-Bond (Protein Donor)	false
O2	NE2	GLN- 27	3.36	175.06	H-Bond (Protein Donor)	false
C2'	CB	GLN- 27	4.19	0	Hydrophobic	false
C5'	CB	GLN- 27	3.61	0	Hydrophobic	false
O2'	O	ILE- 28	2.7	160.53	H-Bond (Ligand Donor)	false
C7	CG2	ILE- 28	3.45	0	Hydrophobic	false
C8	CG2	ILE- 28	3.65	0	Hydrophobic	false
C8	CG2	ILE- 28	3.65	0	Hydrophobic	false
O4	N	ASN- 30	3.11	137.8	H-Bond (Protein Donor)	false
N5	N	ASN- 30	3.1	136.88	H-Bond (Protein Donor)	false
C6	CB	ASN- 30	4.39	0	Hydrophobic	false
O4	OG1	THR- 31	2.93	140.33	H-Bond (Protein Donor)	false
O4	N	THR- 31	3.04	153.28	H-Bond (Protein Donor)	false
N3	O	CYS- 45	3	163.9	H-Bond (Ligand Donor)	false
O2	N	ASN- 47	2.75	154.31	H-Bond (Protein Donor)	false
C5'	CB	ASN- 50	4.21	0	Hydrophobic	false
O1P	N	ASP- 51	2.85	160.29	H-Bond (Protein Donor)	false
O2P	N	THR- 52	2.83	159.55	H-Bond (Protein Donor)	false
O2P	OG1	THR- 52	2.74	152.13	H-Bond (Protein Donor)	false
C8M	CG2	ILE- 76	4.47	0	Hydrophobic	false
C8M	CZ	PHE- 81	3.69	0	Hydrophobic	false
O4'	O	ARG- 82	2.86	152.65	H-Bond (Ligand Donor)	false
O3P	N	SER- 84	2.67	147	H-Bond (Protein Donor)	false
O3P	OG	SER- 84	2.62	164.78	H-Bond (Protein Donor)	false
O3P	NZ	LYS- 89	2.79	160.96	H-Bond (Protein Donor)	false
O3P	NZ	LYS- 89	2.79	0	Ionic (Protein Cationic)	false
C7M	CE1	TYR- 147	3.84	0	Hydrophobic	false
C7M	CE2	TYR- 150	3.47	0	Hydrophobic	false
C8M	CZ	TYR- 150	4.36	0	Hydrophobic	false
C9	C4D	NAP- 3000	3.84	0	Hydrophobic	false
C8M	C5D	NAP- 3000	3.76	0	Hydrophobic	false
O1P	O	HOH- 3042	2.64	179.95	H-Bond (Protein Donor)	false