scPDB - 1umc entry

Protein Data Bank Entry:

PDB ID : 1umc

Resolution :2.400 Å

Experimental Method : X-ray

Deposition Date : 2003-09-25

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	2-oxoisovalerate dehydrogenase subunit alpha	2-oxoisovalerate dehydrogenase subunit beta
ID:	ODBA_THET8	ODBB_THET8
AC:	Q5SLR4	Q5SLR3
Organism:	Thermus thermophilus
Reign:	Bacteria
TaxID:	300852
EC Number:	1.2.4.4

Chains:

Chain Name:	Percentage of Residues within binding site
A	73 %
B	3 %
D	24 %

Ligand binding site composition:

B-Factor:	18.209
Number of residues:	43
Including
Standard Amino Acids:	36
Non Standard Amino Acids:	1
Water Molecules:	6
Cofactors:
Metals:	MG

Cavity properties

Ligandability	Volume (Å3)
0.902	469.125

% Hydrophobic	% Polar
51.80	48.20
According to VolSite

Ligand :

HET Code:	TDP
Formula:	C12H16N4O7P2S
Molecular weight:	422.291 g/mol
DrugBank ID:	DB01987
Buried Surface Area:	76.05 %
Polar Surface area:	225.32 Å2

Number of
H-Bond Acceptors:	10
H-Bond Donors:	1
Rings:	2
Aromatic rings:	2
Anionic atoms:	3
Cationic atoms:	1
Rule of Five Violation:	1
Rotatable Bonds:	8

Mass center Coordinates

X	Y	Z
34.9847	32.4835	58.3476

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
C4A	CD1	LEU- 58	3.42	0	Hydrophobic	false
C5B	CD1	LEU- 58	3.5	0	Hydrophobic	false
N1'	OE2	GLU- 60	2.7	174.28	H-Bond (Ligand Donor)	false
C2A	CB	TYR- 86	3.8	0	Hydrophobic	false
DuAr	DuAr	TYR- 86	3.65	0	Aromatic Face/Face	false
C2A	CG	PRO- 89	3.83	0	Hydrophobic	false
O21	OH	TYR- 94	2.65	169.7	H-Bond (Protein Donor)	false
O22	OH	TYR- 95	2.6	152.54	H-Bond (Protein Donor)	false
O21	CZ	ARG- 96	3.99	0	Ionic (Protein Cationic)	false
O22	CZ	ARG- 96	3.56	0	Ionic (Protein Cationic)	false
O21	NE	ARG- 96	3.03	157.1	H-Bond (Protein Donor)	false
O22	NH2	ARG- 96	2.82	168.88	H-Bond (Protein Donor)	false
O22	NE	ARG- 96	3.44	134.49	H-Bond (Protein Donor)	false
N4'	O	SER- 144	2.96	168.17	H-Bond (Ligand Donor)	false
C2A	CB	PRO- 145	4.22	0	Hydrophobic	false
C2A	CB	ILE- 146	4.27	0	Hydrophobic	false
C5'	CG1	ILE- 146	4.07	0	Hydrophobic	false
S1	CD1	ILE- 146	3.93	0	Hydrophobic	false
C5B	CD1	ILE- 146	3.73	0	Hydrophobic	false
N3'	N	ILE- 146	3.02	169.48	H-Bond (Protein Donor)	false
O12	N	GLY- 176	2.87	163.72	H-Bond (Protein Donor)	false
O13	N	ALA- 177	3.15	139.5	H-Bond (Protein Donor)	false
O21	ND2	ASN- 204	3.17	127.63	H-Bond (Protein Donor)	false
O23	ND2	ASN- 204	2.98	145.85	H-Bond (Protein Donor)	false
C5A	CB	ALA- 207	4.34	0	Hydrophobic	false
S1	CD1	ILE- 208	4.39	0	Hydrophobic	false
C4A	CD1	ILE- 208	3.78	0	Hydrophobic	false
C5A	CG1	ILE- 208	3.47	0	Hydrophobic	false
O12	MG	MG- 1401	2.05	0	Metal Acceptor	false
O23	MG	MG- 1401	2.14	0	Metal Acceptor	false
O21	O	HOH- 1428	2.73	143.03	H-Bond (Protein Donor)	false