scPDB - 1x31 entry

Protein Data Bank Entry:

PDB ID : 1x31

Resolution :2.150 Å

Experimental Method : X-ray

Deposition Date : 2005-04-27

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Subunit alpha of sarocosine oxidase	Subunit beta of sarcosine oxidase
ID:	Q50LF0_9CORY	Q50LF2_9CORY
AC:	Q50LF0	Q50LF2
Organism:	Corynebacterium sp. U-96
Reign:	Bacteria
TaxID:	31944
EC Number:	/

Chains:

Chain Name:	Percentage of Residues within binding site
A	28 %
B	72 %

Ligand binding site composition:

B-Factor:	28.514
Number of residues:	43
Including
Standard Amino Acids:	40
Non Standard Amino Acids:	0
Water Molecules:	3
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.014	587.250

% Hydrophobic	% Polar
43.68	56.32
According to VolSite

Ligand :

HET Code:	FMN
Formula:	C17H19N4O9P
Molecular weight:	454.328 g/mol
DrugBank ID:	DB03247
Buried Surface Area:	71 %
Polar Surface area:	217.05 Å2

Number of
H-Bond Acceptors:	12
H-Bond Donors:	4
Rings:	3
Aromatic rings:	1
Anionic atoms:	2
Cationic atoms:	0
Rule of Five Violation:	1
Rotatable Bonds:	7

Mass center Coordinates

X	Y	Z
-15.345	94.1181	26.3957

Binding mode :

What is Poseview ?

2D View
3D View

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
O4'	O	ALA- 62	2.84	165.22	H-Bond (Ligand Donor)	false
C5'	CG	ARG- 63	4.35	0	Hydrophobic	false
O2P	NH1	ARG- 63	2.82	154.19	H-Bond (Protein Donor)	false
O2P	CZ	ARG- 63	3.71	0	Ionic (Protein Cationic)	false
C7M	CG2	THR- 66	3.52	0	Hydrophobic	false
C6	CG1	VAL- 251	4.04	0	Hydrophobic	false
C9A	CG1	VAL- 251	4.12	0	Hydrophobic	false
O4	NZ	LYS- 277	3.17	121.57	H-Bond (Protein Donor)	false
C6	CG2	VAL- 281	4.45	0	Hydrophobic	false
C7M	CG1	VAL- 281	4.16	0	Hydrophobic	false
O3'	NE	ARG- 322	2.74	170.49	H-Bond (Protein Donor)	false
O3'	NH2	ARG- 322	3.39	130.07	H-Bond (Protein Donor)	false
O3P	NH2	ARG- 322	2.86	134.82	H-Bond (Protein Donor)	false
O3P	CZ	ARG- 322	3.78	0	Ionic (Protein Cationic)	false
C1'	CD	ARG- 322	4.18	0	Hydrophobic	false
C8M	CZ2	TRP- 324	3.43	0	Hydrophobic	false
C1'	CZ3	TRP- 324	3.66	0	Hydrophobic	false
C9	CH2	TRP- 324	3.3	0	Hydrophobic	false
O2'	NZ	LYS- 509	3.17	150.66	H-Bond (Protein Donor)	false
O4'	NH2	ARG- 510	3.15	142.08	H-Bond (Protein Donor)	false
O4'	NE	ARG- 510	3.46	133.69	H-Bond (Protein Donor)	false
O1P	NH2	ARG- 510	3.5	133.35	H-Bond (Protein Donor)	false
N3	O	THR- 516	2.95	152.94	H-Bond (Ligand Donor)	false
O2	NE2	GLN- 520	2.67	171.79	H-Bond (Protein Donor)	false
O1P	OG1	THR- 548	3.1	156.23	H-Bond (Protein Donor)	false
O2P	CZ	ARG- 550	3.51	0	Ionic (Protein Cationic)	false
O3P	CZ	ARG- 550	3.63	0	Ionic (Protein Cationic)	false
O2P	NH2	ARG- 550	2.71	151.58	H-Bond (Protein Donor)	false
O3P	NE	ARG- 550	2.72	170.37	H-Bond (Protein Donor)	false