scPDB - 2e7z entry

Protein Data Bank Entry:

PDB ID : 2e7z

Resolution :1.260 Å

Experimental Method : X-ray

Deposition Date : 2007-01-15

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Acetylene hydratase
ID:	AHY_PELAE
AC:	Q71EW5
Organism:	Pelobacter acetylenicus
Reign:	Bacteria
TaxID:	29542
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	10.142
Number of residues:	68
Including
Standard Amino Acids:	60
Non Standard Amino Acids:	1
Water Molecules:	7
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.633	320.625

% Hydrophobic	% Polar
50.53	49.47
According to VolSite

Ligand :

HET Code:	MGD
Formula:	C20H24N10O13P2S2
Molecular weight:	738.541 g/mol
DrugBank ID:	-
Buried Surface Area:	72.1 %
Polar Surface area:	440.93 Å2

Number of
H-Bond Acceptors:	22
H-Bond Donors:	10
Rings:	6
Aromatic rings:	1
Anionic atoms:	2
Cationic atoms:	0
Rule of Five Violation:	3
Rotatable Bonds:	9

Mass center Coordinates

X	Y	Z
46.6377	77.1082	27.5543

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
O2A	OG1	THR- 111	2.64	153.5	H-Bond (Protein Donor)	false
O1A	ND2	ASN- 114	2.93	151.73	H-Bond (Protein Donor)	false
C23	CB	ALA- 137	3.81	0	Hydrophobic	false
C11	CB	ALA- 137	3.49	0	Hydrophobic	false
C23	CE	MET- 140	4.42	0	Hydrophobic	false
C14	CE	MET- 299	3.62	0	Hydrophobic	false
C1'	CB	ALA- 416	4.28	0	Hydrophobic	false
O5'	N	ASN- 418	3.01	159.77	H-Bond (Protein Donor)	false
C3'	CB	ASN- 418	4.4	0	Hydrophobic	false
N22	O	GLY- 422	2.87	169.21	H-Bond (Ligand Donor)	false
N19	O	TYR- 423	2.82	160.94	H-Bond (Ligand Donor)	false
N2	O	TYR- 442	3.16	161.75	H-Bond (Ligand Donor)	false
O3'	OD2	ASP- 443	2.75	174.32	H-Bond (Ligand Donor)	false
O3'	OD1	ASP- 443	3.42	127.52	H-Bond (Ligand Donor)	false
O2'	OD1	ASP- 443	2.65	158.07	H-Bond (Ligand Donor)	false
O6	NH1	ARG- 465	3.12	139.5	H-Bond (Protein Donor)	false
O6	NH2	ARG- 465	2.86	154.66	H-Bond (Protein Donor)	false
O17	NH2	ARG- 606	3.31	134.62	H-Bond (Protein Donor)	false
O17	NH1	ARG- 606	2.9	154.57	H-Bond (Protein Donor)	false
C10	CG	GLN- 612	3.66	0	Hydrophobic	false
O2B	N	SER- 613	2.89	154.68	H-Bond (Protein Donor)	false
O2B	OG	SER- 613	2.6	175.49	H-Bond (Protein Donor)	false
C3'	SG	CYS- 614	3.52	0	Hydrophobic	false
N18	OD2	ASP- 699	2.85	148.25	H-Bond (Ligand Donor)	false
N19	OD2	ASP- 699	3.05	137.12	H-Bond (Ligand Donor)	false
O17	O	HOH- 1048	2.7	179.94	H-Bond (Protein Donor)	false
O6	O	HOH- 1079	2.91	149.62	H-Bond (Protein Donor)	false