scPDB - 4h49 entry

Protein Data Bank Entry:

PDB ID : 4h49

Resolution :2.160 Å

Experimental Method : X-ray

Deposition Date : 2012-09-17

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Macrophage metalloelastase
ID:	MMP12_HUMAN
AC:	P39900
Organism:	Homo sapiens
Reign:	Eukaryota
TaxID:	9606
EC Number:	3.4.24.65

Chains:

Chain Name:	Percentage of Residues within binding site
A	49 %
B	51 %

Ligand binding site composition:

B-Factor:	16.336
Number of residues:	56
Including
Standard Amino Acids:	54
Non Standard Amino Acids:	2
Water Molecules:	0
Cofactors:
Metals:	ZN ZN

Cavity properties

Ligandability	Volume (Å3)
0.214	2571.750

% Hydrophobic	% Polar
48.82	51.18
According to VolSite

Ligand :

HET Code:	L29
Formula:	C46H52N6O10S2
Molecular weight:	913.069 g/mol
DrugBank ID:	-
Buried Surface Area:	64.83 %
Polar Surface area:	248.37 Å2

Number of
H-Bond Acceptors:	10
H-Bond Donors:	6
Rings:	5
Aromatic rings:	5
Anionic atoms:	0
Cationic atoms:	0
Rule of Five Violation:	4
Rotatable Bonds:	20

Mass center Coordinates

X	Y	Z
3.89347	-11.5233	27.6713

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
C20	CG1	ILE- 180	3.94	0	Hydrophobic	false
C58	CG1	ILE- 180	4.17	0	Hydrophobic	false
O15	N	LEU- 181	2.77	145.59	H-Bond (Protein Donor)	false
O43	N	LEU- 181	2.64	159.17	H-Bond (Protein Donor)	false
C49	CD1	LEU- 181	4.4	0	Hydrophobic	false
C5A	CB	LEU- 181	4.05	0	Hydrophobic	false
C12	CD1	LEU- 181	4.19	0	Hydrophobic	false
O15	N	ALA- 182	3.3	163.29	H-Bond (Protein Donor)	false
O43	N	ALA- 182	3.3	167.83	H-Bond (Protein Donor)	false
N22	O	ALA- 182	2.73	159.77	H-Bond (Ligand Donor)	false
N61	O	ALA- 182	2.81	163.32	H-Bond (Ligand Donor)	false
C19	CB	HIS- 183	4.17	0	Hydrophobic	false
C59	CB	HIS- 183	4.17	0	Hydrophobic	false
C5	CB	LEU- 214	3.99	0	Hydrophobic	false
C54	CB	LEU- 214	3.97	0	Hydrophobic	false
C12	CG2	THR- 215	4.32	0	Hydrophobic	false
C49	CG2	THR- 215	4.34	0	Hydrophobic	false
C55	CB	THR- 215	4.27	0	Hydrophobic	false
C6	CB	THR- 215	4.21	0	Hydrophobic	false
C12	CB	HIS- 218	4.46	0	Hydrophobic	false
C49	CB	HIS- 218	4.31	0	Hydrophobic	false
C50	CB	HIS- 218	3.74	0	Hydrophobic	false
C55	CB	HIS- 218	3.86	0	Hydrophobic	false
C1	CB	HIS- 218	3.77	0	Hydrophobic	false
O22	OE1	GLU- 219	2.78	147.06	H-Bond (Ligand Donor)	false
O22	OE2	GLU- 219	2.67	139.74	H-Bond (Ligand Donor)	false
C4	CG2	VAL- 235	4.18	0	Hydrophobic	false
C53	CG2	VAL- 235	3.93	0	Hydrophobic	false
C20	CZ	PHE- 237	4.03	0	Hydrophobic	false
C58	CZ	PHE- 237	4.09	0	Hydrophobic	false
C24	CB	PRO- 238	4.38	0	Hydrophobic	false
C39	CB	PRO- 238	4.15	0	Hydrophobic	false
C34	CG	PRO- 238	3.45	0	Hydrophobic	false
C33	CG	PRO- 238	3.76	0	Hydrophobic	false
C33	CG	PRO- 238	3.8	0	Hydrophobic	false
C34	CG	PRO- 238	3.5	0	Hydrophobic	false
O42	OG1	THR- 239	3.22	164.56	H-Bond (Protein Donor)	false
C8	CB	TYR- 240	4.35	0	Hydrophobic	false
C5	CD1	TYR- 240	3.45	0	Hydrophobic	false
C6	CB	TYR- 240	4.17	0	Hydrophobic	false
C55	CB	TYR- 240	4.28	0	Hydrophobic	false
O22	ZN	ZN- 301	2.49	0	Metal Acceptor	false
O23	ZN	ZN- 301	2.17	0	Metal Acceptor	false
O61	ZN	ZN- 602	2.3	0	Metal Acceptor	false
O62	ZN	ZN- 602	2.06	0	Metal Acceptor	false