scPDB - 3mpj entry

Protein Data Bank Entry:

PDB ID : 3mpj

Resolution :2.100 Å

Experimental Method : X-ray

Deposition Date : 2010-04-27

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Glutaryl-CoA dehydrogenase
ID:	ACD_DESML
AC:	C3UVB0
Organism:	Desulfococcus multivorans
Reign:	Bacteria
TaxID:	897
EC Number:	1.3.99.32

Chains:

Chain Name:	Percentage of Residues within binding site
D	63 %
E	35 %
G	2 %

Ligand binding site composition:

B-Factor:	31.444
Number of residues:	58
Including
Standard Amino Acids:	54
Non Standard Amino Acids:	0
Water Molecules:	4
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.808	1694.250

% Hydrophobic	% Polar
46.02	53.98
According to VolSite

Ligand :

HET Code:	FAD
Formula:	C27H31N9O15P2
Molecular weight:	783.534 g/mol
DrugBank ID:	DB03147
Buried Surface Area:	71.11 %
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
67.7436	60.9936	-4.5294

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
N3	O	PHE- 126	2.9	150.14	H-Bond (Ligand Donor)	false
O2	N	ILE- 128	3.04	133.41	H-Bond (Protein Donor)	false
N1	OG1	THR- 129	2.64	168.72	H-Bond (Protein Donor)	false
O2	N	THR- 129	2.95	167.42	H-Bond (Protein Donor)	false
C1'	CB	THR- 129	4.02	0	Hydrophobic	false
O4'	OG1	THR- 129	3.19	150.55	H-Bond (Ligand Donor)	false
O1A	OG	SER- 135	2.6	153.41	H-Bond (Protein Donor)	false
O1A	N	SER- 135	2.77	154.73	H-Bond (Protein Donor)	false
C8M	CE3	TRP- 159	4.25	0	Hydrophobic	false
C1'	CB	TRP- 159	3.74	0	Hydrophobic	false
C9	CB	TRP- 159	3.63	0	Hydrophobic	false
O4	N	SER- 161	2.91	160.31	H-Bond (Protein Donor)	false
O4	OG	SER- 161	3.22	147.34	H-Bond (Protein Donor)	false
N5	OG	SER- 161	2.97	136.27	H-Bond (Protein Donor)	false
C7M	CD	LYS- 204	3.78	0	Hydrophobic	false
C6	CG2	THR- 212	3.84	0	Hydrophobic	false
O2A	NE	ARG- 271	2.83	148.51	H-Bond (Protein Donor)	false
O2A	NH2	ARG- 271	2.81	146.15	H-Bond (Protein Donor)	false
O2P	NH2	ARG- 271	3.28	120.06	H-Bond (Protein Donor)	false
O2A	CZ	ARG- 271	3.26	0	Ionic (Protein Cationic)	false
C4B	CD1	ILE- 278	3.8	0	Hydrophobic	false
DuAr	DuAr	PHE- 281	3.89	0	Aromatic Face/Face	false
N1A	NE2	GLN- 282	2.75	167.52	H-Bond (Protein Donor)	false
O4B	ND2	ASN- 284	3.35	174.73	H-Bond (Protein Donor)	false
O3B	O	ARG- 340	2.54	130.19	H-Bond (Ligand Donor)	false
C3'	CB	ALA- 344	4.28	0	Hydrophobic	false
C8M	CB	ALA- 344	3.71	0	Hydrophobic	false
O1P	N	ALA- 344	2.82	177.3	H-Bond (Protein Donor)	false
C7M	CD2	TYR- 347	4.42	0	Hydrophobic	false
C7M	CG2	THR- 362	4.29	0	Hydrophobic	false
C8M	SD	MET- 365	4.06	0	Hydrophobic	false
C2'	CB	VAL- 366	4.2	0	Hydrophobic	false
C7	CG1	VAL- 366	4.05	0	Hydrophobic	false
C8M	CG1	VAL- 366	3.39	0	Hydrophobic	false
O2'	N	GLU- 367	3.34	167.25	H-Bond (Protein Donor)	false
C2B	CB	SER- 369	4.33	0	Hydrophobic	false
N3A	ND2	ASN- 371	3.16	161.42	H-Bond (Protein Donor)	false
C2B	CD1	ILE- 372	4.33	0	Hydrophobic	false
O4	O	HOH- 7422	2.81	179.97	H-Bond (Protein Donor)	false
O2'	O	HOH- 7690	3.39	179.96	H-Bond (Protein Donor)	false