scPDB - 3gcu entry

Protein Data Bank Entry:

PDB ID : 3gcu

Resolution :2.100 Å

Experimental Method : X-ray

Deposition Date : 2009-02-22

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:	30.004
Number of residues:	36
Including
Standard Amino Acids:	36
Non Standard Amino Acids:	0
Water Molecules:	0
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.498	799.875

% Hydrophobic	% Polar
43.04	56.96
According to VolSite

Ligand :

HET Code:	R48
Formula:	C29H30N8O
Molecular weight:	506.601 g/mol
DrugBank ID:	-
Buried Surface Area:	66.37 %
Polar Surface area:	122.78 Å2

Number of
H-Bond Acceptors:	6
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
19.0756	4.7	-35.4245

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
C1M	CG2	VAL- 30	4.18	0	Hydrophobic	false
C1S	CG1	VAL- 38	3.98	0	Hydrophobic	false
C5	CB	ALA- 51	3.96	0	Hydrophobic	false
C1J	CB	ALA- 51	4.11	0	Hydrophobic	false
C1I	CD	LYS- 53	3.78	0	Hydrophobic	false
C1Q	CD	LYS- 53	4.03	0	Hydrophobic	false
C1G	CB	LYS- 53	3.63	0	Hydrophobic	false
C1A	CB	ARG- 67	3.89	0	Hydrophobic	false
C1K	CG	ARG- 70	4.38	0	Hydrophobic	false
N1W	OE2	GLU- 71	2.9	157.69	H-Bond (Ligand Donor)	false
N1X	OE2	GLU- 71	3.08	150.02	H-Bond (Ligand Donor)	false
C1K	CB	GLU- 71	3.56	0	Hydrophobic	false
C1N	CG	GLU- 71	3.82	0	Hydrophobic	false
C1C	CD2	LEU- 74	4.14	0	Hydrophobic	false
C1D	CD2	LEU- 74	4.13	0	Hydrophobic	false
C1N	CD2	LEU- 74	4.11	0	Hydrophobic	false
C1I	CD1	LEU- 75	4.08	0	Hydrophobic	false
C1C	CD2	LEU- 75	4.06	0	Hydrophobic	false
C1C	CG	MET- 78	4.01	0	Hydrophobic	false
C1C	CG1	VAL- 83	3.89	0	Hydrophobic	false
C1C	CG2	ILE- 84	4.47	0	Hydrophobic	false
C1I	CB	LEU- 104	4.16	0	Hydrophobic	false
C1G	CG2	THR- 106	3.62	0	Hydrophobic	false
C1P	CD1	LEU- 108	3.81	0	Hydrophobic	false
N3	N	MET- 109	2.95	170.03	H-Bond (Protein Donor)	false
C1D	CD1	ILE- 141	4.47	0	Hydrophobic	false
C1B	CD1	ILE- 141	4.2	0	Hydrophobic	false
C1D	CG2	ILE- 146	4.14	0	Hydrophobic	false
C1B	CG2	ILE- 166	3.87	0	Hydrophobic	false
O1F	N	ASP- 168	3.28	167.91	H-Bond (Protein Donor)	false
C1O	CB	ASP- 168	4.42	0	Hydrophobic	false
C1S	CD1	PHE- 169	3.33	0	Hydrophobic	false
C5	CE1	PHE- 169	3.41	0	Hydrophobic	false