scPDB - 3hv4 entry

Protein Data Bank Entry:

PDB ID : 3hv4

Resolution :2.600 Å

Experimental Method : X-ray

Deposition Date : 2009-06-15

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Mitogen-activated protein kinase 14
ID:	MK14_HUMAN
AC:	Q16539
Organism:	Homo sapiens
Reign:	Eukaryota
TaxID:	9606
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	16.037
Number of residues:	39
Including
Standard Amino Acids:	39
Non Standard Amino Acids:	0
Water Molecules:	0
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.376	833.625

% Hydrophobic	% Polar
44.94	55.06
According to VolSite

Ligand :

HET Code:	L51
Formula:	C30H31N7O
Molecular weight:	505.613 g/mol
DrugBank ID:	-
Buried Surface Area:	65.06 %
Polar Surface area:	109.89 Å2

Number of
H-Bond Acceptors:	5
H-Bond Donors:	4
Rings:	5
Aromatic rings:	5
Anionic atoms:	0
Cationic atoms:	0
Rule of Five Violation:	2
Rotatable Bonds:	6

Mass center Coordinates

X	Y	Z
14.1855	4.62432	36.2671

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
CAN	CG2	VAL- 30	3.68	0	Hydrophobic	false
CAT	CG2	VAL- 38	3.91	0	Hydrophobic	false
CBB	CB	VAL- 38	4.37	0	Hydrophobic	false
CBJ	CG1	VAL- 38	4.1	0	Hydrophobic	false
CAJ	CB	ALA- 51	4.28	0	Hydrophobic	false
CAM	CB	ALA- 51	3.43	0	Hydrophobic	false
CAI	CD	LYS- 53	3.9	0	Hydrophobic	false
CAR	CD	LYS- 53	4.19	0	Hydrophobic	false
CAG	CB	LYS- 53	3.65	0	Hydrophobic	false
CAA	CB	ARG- 67	3.93	0	Hydrophobic	false
NAW	OE1	GLU- 71	2.5	151.75	H-Bond (Ligand Donor)	false
NAX	OE1	GLU- 71	2.72	141.83	H-Bond (Ligand Donor)	false
CAK	CB	GLU- 71	3.53	0	Hydrophobic	false
CBE	CG	GLU- 71	3.75	0	Hydrophobic	false
CAD	CD2	LEU- 74	4.21	0	Hydrophobic	false
CAB	CD2	LEU- 74	4.3	0	Hydrophobic	false
CAO	CD2	LEU- 74	4.03	0	Hydrophobic	false
CAI	CD1	LEU- 75	4.13	0	Hydrophobic	false
CAD	CD2	LEU- 75	4	0	Hydrophobic	false
CAD	CG	MET- 78	3.94	0	Hydrophobic	false
CAD	CG1	VAL- 83	4.06	0	Hydrophobic	false
CAI	CB	LEU- 104	4.33	0	Hydrophobic	false
CAG	CG2	THR- 106	3.73	0	Hydrophobic	false
CAQ	CD1	LEU- 108	4.42	0	Hydrophobic	false
NAU	N	MET- 109	3.45	157.6	H-Bond (Protein Donor)	false
CAM	CG	MET- 109	4.38	0	Hydrophobic	false
CAC	CD1	ILE- 141	4.11	0	Hydrophobic	false
CAD	CD1	ILE- 141	4.43	0	Hydrophobic	false
CAB	CD1	ILE- 141	4.35	0	Hydrophobic	false
CAB	CG2	ILE- 146	4.42	0	Hydrophobic	false
CAC	CG2	ILE- 166	4.01	0	Hydrophobic	false
CBF	CD1	LEU- 167	4.1	0	Hydrophobic	false
CAR	CD1	LEU- 167	4.31	0	Hydrophobic	false
OAF	N	ASP- 168	3.39	162.78	H-Bond (Protein Donor)	false
CAP	CB	ASP- 168	4.12	0	Hydrophobic	false
CAN	CE1	PHE- 169	3.38	0	Hydrophobic	false