scPDB - 4h6u entry

Protein Data Bank Entry:

PDB ID : 4h6u

Resolution :2.450 Å

Experimental Method : X-ray

Deposition Date : 2012-09-19

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Alpha-tubulin N-acetyltransferase 1
ID:	ATAT_DANRE
AC:	Q6PH17
Organism:	Danio rerio
Reign:	Eukaryota
TaxID:	7955
EC Number:	/

Chains:

Chain Name:	Percentage of Residues within binding site
A	3 %
B	97 %

Ligand binding site composition:

B-Factor:	44.174
Number of residues:	36
Including
Standard Amino Acids:	35
Non Standard Amino Acids:	0
Water Molecules:	1
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.333	479.250

% Hydrophobic	% Polar
48.59	51.41
According to VolSite

Ligand :

HET Code:	ACO
Formula:	C23H34N7O17P3S
Molecular weight:	805.539 g/mol
DrugBank ID:	-
Buried Surface Area:	62.58 %
Polar Surface area:	429.68 Å2

Number of
H-Bond Acceptors:	22
H-Bond Donors:	5
Rings:	3
Aromatic rings:	2
Anionic atoms:	4
Cationic atoms:	0
Rule of Five Violation:	2
Rotatable Bonds:	20

Mass center Coordinates

X	Y	Z
65.776	50.3707	86.0748

Binding mode :

What is Poseview ?

2D View
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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
CCP	CE2	PHE- 118	4.47	0	Hydrophobic	false
CDP	CD2	PHE- 118	4.5	0	Hydrophobic	false
CEP	CD2	PHE- 118	3.65	0	Hydrophobic	false
C2P	CB	PHE- 118	3.9	0	Hydrophobic	false
CEP	CG2	VAL- 120	4.21	0	Hydrophobic	false
CAP	CB	VAL- 120	4.42	0	Hydrophobic	false
CAP	CG	GLN- 125	3.77	0	Hydrophobic	false
O8A	NH1	ARG- 126	3.28	161.07	H-Bond (Protein Donor)	false
O5A	N	ARG- 126	3.12	164.03	H-Bond (Protein Donor)	false
DuAr	CZ	ARG- 126	3.83	162.57	Pi/Cation	false
O2A	N	GLY- 128	2.98	141.52	H-Bond (Protein Donor)	false
O4A	N	GLY- 130	2.83	152.78	H-Bond (Protein Donor)	false
O1A	N	SER- 131	2.92	155.87	H-Bond (Protein Donor)	false
CH3	CB	PRO- 153	3.97	0	Hydrophobic	false
S1P	CB	SER- 154	4.01	0	Hydrophobic	false
CDP	CB	LYS- 156	4.24	0	Hydrophobic	false
C6P	CD	LYS- 156	3.66	0	Hydrophobic	false
CDP	CB	PHE- 157	3.92	0	Hydrophobic	false
C2P	CB	PHE- 157	4.09	0	Hydrophobic	false
S1P	CD2	PHE- 157	3.8	0	Hydrophobic	false
CH3	CD2	PHE- 157	3.53	0	Hydrophobic	false
N3A	OG	SER- 159	3.37	150.08	H-Bond (Protein Donor)	false
O2B	OG	SER- 159	2.82	150.61	H-Bond (Ligand Donor)	false
C2B	CB	SER- 159	3.96	0	Hydrophobic	false
C1B	CB	PHE- 160	3.95	0	Hydrophobic	false
CCP	CD2	PHE- 160	3.77	0	Hydrophobic	false
C4B	CD2	PHE- 160	4.19	0	Hydrophobic	false
C2B	CD	LYS- 163	4.04	0	Hydrophobic	false
O7A	NZ	LYS- 163	2.85	165.39	H-Bond (Protein Donor)	false
O7A	NZ	LYS- 163	2.85	0	Ionic (Protein Cationic)	false
O9A	NZ	LYS- 163	3.49	0	Ionic (Protein Cationic)	false
O4A	O	HOH- 305	2.66	143.94	H-Bond (Protein Donor)	false