scPDB - 1ib0 entry

Protein Data Bank Entry:

PDB ID : 1ib0

Resolution :2.300 Å

Experimental Method : X-ray

Deposition Date : 2001-03-26

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	NADH-cytochrome b5 reductase 3
ID:	NB5R3_RAT
AC:	P20070
Organism:	Rattus norvegicus
Reign:	Eukaryota
TaxID:	10116
EC Number:	1.6.2.2

Chains:

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

Ligand binding site composition:

B-Factor:	20.565
Number of residues:	42
Including
Standard Amino Acids:	40
Non Standard Amino Acids:	1
Water Molecules:	1
Cofactors:	NAD
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.743	573.750

% Hydrophobic	% Polar
46.47	53.53
According to VolSite

Ligand :

HET Code:	FAD
Formula:	C27H31N9O15P2
Molecular weight:	783.534 g/mol
DrugBank ID:	DB03147
Buried Surface Area:	62.84 %
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
21.1771	1.64392	31.6465

Binding mode :

What is Poseview ?

2D View
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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
C7M	CB	HIS- 77	4.25	0	Hydrophobic	false
O1A	NE	ARG- 91	3.15	124.97	H-Bond (Protein Donor)	false
O1A	NH2	ARG- 91	3.07	122.63	H-Bond (Protein Donor)	false
O5'	NE	ARG- 91	3.41	143.42	H-Bond (Protein Donor)	false
O1P	NE	ARG- 91	3.04	134.7	H-Bond (Protein Donor)	false
O1A	CZ	ARG- 91	3.44	0	Ionic (Protein Cationic)	false
O1P	CZ	ARG- 91	3.76	0	Ionic (Protein Cationic)	false
C5'	CD	ARG- 91	4.35	0	Hydrophobic	false
C7	CB	PRO- 92	4.23	0	Hydrophobic	false
C8	CG	PRO- 92	3.71	0	Hydrophobic	false
C9	CG	PRO- 92	3.7	0	Hydrophobic	false
O2'	O	PRO- 92	2.92	151.36	H-Bond (Ligand Donor)	false
C2'	CE1	TYR- 93	4.07	0	Hydrophobic	false
N5	N	THR- 94	3.11	136.51	H-Bond (Protein Donor)	false
C6	CB	THR- 94	4.32	0	Hydrophobic	false
N3	O	VAL- 108	2.89	173.34	H-Bond (Ligand Donor)	false
O2	N	LYS- 110	3.27	160.57	H-Bond (Protein Donor)	false
C5'	CE2	TYR- 112	4.34	0	Hydrophobic	false
N6A	O	PHE- 113	2.77	125.12	H-Bond (Ligand Donor)	false
C4B	CE1	PHE- 120	4.41	0	Hydrophobic	false
C1B	CD2	PHE- 120	3.57	0	Hydrophobic	false
O2A	N	LYS- 125	3.12	160.34	H-Bond (Protein Donor)	false
O3P	N	LYS- 125	3.45	137.1	H-Bond (Protein Donor)	false
O1P	N	MET- 126	2.65	154.42	H-Bond (Protein Donor)	false
O2P	N	SER- 127	2.8	159.74	H-Bond (Protein Donor)	false
O2P	OG	SER- 127	2.64	149.76	H-Bond (Protein Donor)	false
O4	OG1	THR- 184	2.83	154	H-Bond (Protein Donor)	false
C6	CG	PRO- 185	3.62	0	Hydrophobic	false
C8M	SG	CYS- 273	4.46	0	Hydrophobic	false
C8	SG	CYS- 273	4.29	0	Hydrophobic	false
C7M	CB	PHE- 300	4.12	0	Hydrophobic	false
C1'	C2D	NAD- 1994	3.5	0	Hydrophobic	false
C9	C2D	NAD- 1994	3.84	0	Hydrophobic	false