scPDB - 1ake entry

Protein Data Bank Entry:

PDB ID : 1ake

Resolution :2.000 Å

Experimental Method : X-ray

Deposition Date : 1991-11-08

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Adenylate kinase
ID:	KAD_ECOLI
AC:	P69441
Organism:	Escherichia coli
Reign:	Bacteria
TaxID:	83333
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	22.566
Number of residues:	44
Including
Standard Amino Acids:	42
Non Standard Amino Acids:	0
Water Molecules:	2
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.112	347.625

% Hydrophobic	% Polar
50.49	49.51
According to VolSite

Ligand :

HET Code:	AP5
Formula:	C20H24N10O22P5
Molecular weight:	911.327 g/mol
DrugBank ID:	DB01717
Buried Surface Area:	68.79 %
Polar Surface area:	543.69 Å2

Number of
H-Bond Acceptors:	30
H-Bond Donors:	6
Rings:	6
Aromatic rings:	4
Anionic atoms:	5
Cationic atoms:	0
Rule of Five Violation:	3
Rotatable Bonds:	16

Mass center Coordinates

X	Y	Z
16.5798	46.3766	20.0894

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
O3B	N	GLY- 10	3.01	143.21	H-Bond (Protein Donor)	false
O1G	N	GLY- 10	3.42	142.88	H-Bond (Protein Donor)	false
O1B	N	ALA- 11	3.05	123.27	H-Bond (Protein Donor)	false
O3A	N	GLY- 12	2.98	137.18	H-Bond (Protein Donor)	false
O1B	N	GLY- 12	3.11	131.05	H-Bond (Protein Donor)	false
O3A	N	LYS- 13	3.38	124.29	H-Bond (Protein Donor)	false
O1B	NZ	LYS- 13	2.78	152.86	H-Bond (Protein Donor)	false
O1B	N	LYS- 13	2.91	169.21	H-Bond (Protein Donor)	false
O2G	NZ	LYS- 13	3.01	137.39	H-Bond (Protein Donor)	false
O1B	NZ	LYS- 13	2.78	0	Ionic (Protein Cationic)	false
O2G	NZ	LYS- 13	3.01	0	Ionic (Protein Cationic)	false
O2B	N	GLY- 14	2.7	163.57	H-Bond (Protein Donor)	false
O1A	N	THR- 15	2.85	150.3	H-Bond (Protein Donor)	false
O1A	OG1	THR- 15	2.71	159.08	H-Bond (Protein Donor)	false
O1D	CZ	ARG- 36	3.72	0	Ionic (Protein Cationic)	false
C4F	CB	ARG- 119	4.12	0	Hydrophobic	false
DuAr	CZ	ARG- 119	3.68	3.64	Pi/Cation	false
O2A	NH1	ARG- 123	2.91	149.72	H-Bond (Protein Donor)	false
O3B	NH1	ARG- 123	3.27	137.35	H-Bond (Protein Donor)	false
O3G	NH1	ARG- 123	3.21	139.24	H-Bond (Protein Donor)	false
O2A	CZ	ARG- 123	3.99	0	Ionic (Protein Cationic)	false
O2D	CZ	ARG- 123	3.33	0	Ionic (Protein Cationic)	false
C3F	CD	ARG- 123	3.8	0	Hydrophobic	false
C4F	CD	ARG- 123	4.24	0	Hydrophobic	false
C3F	CG2	VAL- 132	3.7	0	Hydrophobic	false
O3F	O	TYR- 133	2.96	159.96	H-Bond (Ligand Donor)	false
C2F	CB	HIS- 134	4.13	0	Hydrophobic	false
O1D	CZ	ARG- 156	3.18	0	Ionic (Protein Cationic)	false
O2D	CZ	ARG- 156	2.55	0	Ionic (Protein Cationic)	false
N6A	O	LYS- 200	2.77	170.71	H-Bond (Ligand Donor)	false
O2F	O	HOH- 304	2.66	174.31	H-Bond (Ligand Donor)	false