scPDB - 3ab1 entry

Protein Data Bank Entry:

PDB ID : 3ab1

Resolution :2.390 Å

Experimental Method : X-ray

Deposition Date : 2009-11-30

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Ferredoxin--NADP reductase
ID:	FENR_CHLTE
AC:	Q8KCB2
Organism:	Chlorobium tepidum
Reign:	Bacteria
TaxID:	194439
EC Number:	1.18.1.2

Chains:

Chain Name:	Percentage of Residues within binding site
A	93 %
B	7 %

Ligand binding site composition:

B-Factor:	38.275
Number of residues:	62
Including
Standard Amino Acids:	58
Non Standard Amino Acids:	0
Water Molecules:	4
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.760	445.500

% Hydrophobic	% Polar
48.48	51.52
According to VolSite

Ligand :

HET Code:	FAD
Formula:	C27H31N9O15P2
Molecular weight:	783.534 g/mol
DrugBank ID:	DB03147
Buried Surface Area:	77.64 %
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
66.5844	39.6654	76.9583

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
C4'	CG	PRO- 24	4.1	0	Hydrophobic	false
O1P	OG1	THR- 25	2.83	157.44	H-Bond (Protein Donor)	false
O2P	N	THR- 25	3.18	146.75	H-Bond (Protein Donor)	false
O2P	OG1	THR- 25	3.15	122.31	H-Bond (Protein Donor)	false
O3B	OE2	GLU- 44	2.86	171.73	H-Bond (Ligand Donor)	false
O2B	OE1	GLU- 44	2.82	157.88	H-Bond (Ligand Donor)	false
N3A	N	SER- 45	3.16	127.49	H-Bond (Protein Donor)	false
O1A	N	GLN- 52	2.93	175.96	H-Bond (Protein Donor)	false
O2A	NE2	GLN- 52	3.21	155.02	H-Bond (Protein Donor)	false
C2'	CD1	LEU- 53	4.42	0	Hydrophobic	false
C4'	CD1	LEU- 53	4.03	0	Hydrophobic	false
C8M	CD1	LEU- 56	3.81	0	Hydrophobic	false
C7M	CD2	TYR- 57	3.81	0	Hydrophobic	false
C8M	CE2	TYR- 57	4.37	0	Hydrophobic	false
O2'	OH	TYR- 57	2.7	176.5	H-Bond (Protein Donor)	false
DuAr	DuAr	TYR- 57	3.91	0	Aromatic Face/Face	false
N3	OD2	ASP- 64	2.75	172.97	H-Bond (Ligand Donor)	false
N6A	O	VAL- 97	2.96	156.51	H-Bond (Ligand Donor)	false
N1A	N	VAL- 97	2.86	160.02	H-Bond (Protein Donor)	false
C3B	CE2	PHE- 132	3.75	0	Hydrophobic	false
O3'	OD1	ASP- 298	2.74	168.92	H-Bond (Ligand Donor)	false
O3'	OD2	ASP- 298	3.31	132.15	H-Bond (Ligand Donor)	false
C5'	CB	ASP- 298	4.25	0	Hydrophobic	false
O1P	N	ASP- 298	3	152.43	H-Bond (Protein Donor)	false
O2	N	ILE- 309	2.93	165.65	H-Bond (Protein Donor)	false
C4'	CG1	ILE- 309	4	0	Hydrophobic	false
C6	CB	PHE- 337	4.12	0	Hydrophobic	false
C8M	CE2	PHE- 337	4.48	0	Hydrophobic	false
C9A	CB	PHE- 337	4.34	0	Hydrophobic	false
C1'	CE1	PHE- 337	3.68	0	Hydrophobic	false
DuAr	DuAr	PHE- 337	3.94	0	Aromatic Face/Face	false
O4	OG	SER- 338	2.85	153.57	H-Bond (Protein Donor)	false
O4	N	SER- 339	3.17	151.03	H-Bond (Protein Donor)	false
O4	OG	SER- 339	3.24	125.86	H-Bond (Protein Donor)	false
N5	OG	SER- 339	2.74	148.61	H-Bond (Protein Donor)	false
C6	CG2	VAL- 340	4.47	0	Hydrophobic	false
O2A	O	HOH- 414	2.54	122	H-Bond (Protein Donor)	false
O1P	O	HOH- 420	3.17	179.96	H-Bond (Protein Donor)	false
O2P	O	HOH- 421	2.5	170.33	H-Bond (Protein Donor)	false
O3B	O	HOH- 433	3.21	121.16	H-Bond (Protein Donor)	false