scPDB - 4h8n entry

Protein Data Bank Entry:

PDB ID : 4h8n

Resolution :1.800 Å

Experimental Method : X-ray

Deposition Date : 2012-09-23

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	NADPH-dependent conjugated polyketone reductase C2
ID:	CPRC2_CANPA
AC:	Q76L36
Organism:	Candida parapsilosis
Reign:	Eukaryota
TaxID:	5480
EC Number:	/

Chains:

Chain Name:	Percentage of Residues within binding site
A	19 %
B	81 %

Ligand binding site composition:

B-Factor:	20.510
Number of residues:	54
Including
Standard Amino Acids:	53
Non Standard Amino Acids:	1
Water Molecules:	0
Cofactors:	NDP
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.750	610.875

% Hydrophobic	% Polar
46.41	53.59
According to VolSite

Ligand :

HET Code:	NDP
Formula:	C21H26N7O17P3
Molecular weight:	741.389 g/mol
DrugBank ID:	DB02338
Buried Surface Area:	78.75 %
Polar Surface area:	404.9 Å2

Number of
H-Bond Acceptors:	22
H-Bond Donors:	5
Rings:	5
Aromatic rings:	2
Anionic atoms:	4
Cationic atoms:	0
Rule of Five Violation:	2
Rotatable Bonds:	13

Mass center Coordinates

X	Y	Z
16.3553	42.0615	37.2417

Binding mode :

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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
O3D	N	GLY- 26	3.01	140.93	H-Bond (Protein Donor)	false
O1N	OG1	THR- 27	3.18	176.78	H-Bond (Protein Donor)	false
C3D	CG2	THR- 27	4.02	0	Hydrophobic	false
C5N	CG2	THR- 27	3.93	0	Hydrophobic	false
O3D	OG1	THR- 27	2.94	152.67	H-Bond (Ligand Donor)	false
O2B	NZ	LYS- 28	3.13	129.67	H-Bond (Protein Donor)	false
O1X	NZ	LYS- 28	2.85	154.08	H-Bond (Protein Donor)	false
O3X	NZ	LYS- 28	3.43	145.12	H-Bond (Protein Donor)	false
O1X	NZ	LYS- 28	3.87	0	Ionic (Protein Cationic)	false
O1X	NZ	LYS- 28	2.85	0	Ionic (Protein Cationic)	false
O3X	NZ	LYS- 28	3.43	0	Ionic (Protein Cationic)	false
O2D	OD2	ASP- 58	2.7	169.59	H-Bond (Ligand Donor)	false
C2D	CZ	TYR- 63	3.92	0	Hydrophobic	false
N7N	OG	SER- 161	2.58	127.99	H-Bond (Ligand Donor)	false
O7N	ND2	ASN- 162	3.15	172.4	H-Bond (Protein Donor)	false
N7N	OE1	GLN- 186	3.04	173.17	H-Bond (Ligand Donor)	false
DuAr	DuAr	PHE- 214	3.62	0	Aromatic Face/Face	false
C5N	CB	PHE- 214	3.99	0	Hydrophobic	false
O2N	OG	SER- 215	2.64	163.96	H-Bond (Protein Donor)	false
O1A	N	LEU- 217	2.82	151.43	H-Bond (Protein Donor)	false
C4B	CB	ALA- 221	3.94	0	Hydrophobic	false
C1B	CB	ALA- 221	4.02	0	Hydrophobic	false
O2N	CZ	ARG- 222	3.96	0	Ionic (Protein Cationic)	false
O2N	NH2	ARG- 222	3.33	145.1	H-Bond (Protein Donor)	false
C4N	CG	GLU- 224	3.87	0	Hydrophobic	false
C4D	CG1	VAL- 259	3.78	0	Hydrophobic	false
O2A	N	THR- 261	3.25	142.91	H-Bond (Protein Donor)	false
C5B	CG2	THR- 261	3.69	0	Hydrophobic	false
C3B	CG2	THR- 261	4.43	0	Hydrophobic	false
C5D	CG2	THR- 261	4.28	0	Hydrophobic	false
O2X	OG	SER- 262	2.67	162.19	H-Bond (Protein Donor)	false
O3X	OG	SER- 262	3.38	131.93	H-Bond (Protein Donor)	false
O3X	N	SER- 263	2.8	148.95	H-Bond (Protein Donor)	false
O3X	OG	SER- 263	3.34	161.4	H-Bond (Protein Donor)	false
O2X	NH1	ARG- 267	2.76	155.37	H-Bond (Protein Donor)	false
O2X	CZ	ARG- 267	3.79	0	Ionic (Protein Cationic)	false
DuAr	CZ	ARG- 267	3.85	159.4	Pi/Cation	false