scPDB - 1hbn entry

Protein Data Bank Entry:

PDB ID : 1hbn

Resolution :1.160 Å

Experimental Method : X-ray

Deposition Date : 2001-04-20

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Methyl-coenzyme M reductase I subunit alpha	Methyl-coenzyme M reductase I subunit beta
ID:	MCRA_METTM	MCRB_METTM
AC:	P11558	P11560
Organism:	Methanothermobacter marburgensis
Reign:	Archaea
TaxID:	79929
EC Number:	2.8.4.1

Chains:

Chain Name:	Percentage of Residues within binding site
A	19 %
D	47 %
E	34 %

Ligand binding site composition:

B-Factor:	12.045
Number of residues:	33
Including
Standard Amino Acids:	29
Non Standard Amino Acids:	4
Water Molecules:	0
Cofactors:
Metals:	NA

Cavity properties

Ligandability	Volume (Å3)
0.278	408.375

% Hydrophobic	% Polar
55.37	44.63
According to VolSite

Ligand :

HET Code:	TP7
Formula:	C11H19NO7PS
Molecular weight:	340.310 g/mol
DrugBank ID:	-
Buried Surface Area:	82.03 %
Polar Surface area:	190.26 Å2

Number of
H-Bond Acceptors:	8
H-Bond Donors:	2
Rings:	0
Aromatic rings:	0
Anionic atoms:	3
Cationic atoms:	0
Rule of Five Violation:	0
Rotatable Bonds:	11

Mass center Coordinates

X	Y	Z
24.711	38.184	-47.9687

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
O	CZ	ARG- 225	3.9	0	Ionic (Protein Cationic)	false
OXT	CZ	ARG- 225	3.55	0	Ionic (Protein Cationic)	false
O	NH1	ARG- 225	3.08	167.1	H-Bond (Protein Donor)	false
OXT	NE	ARG- 225	2.78	175.57	H-Bond (Protein Donor)	false
OXT	NH1	ARG- 225	3.48	128.36	H-Bond (Protein Donor)	false
O3P	NZ	LYS- 256	2.84	167.95	H-Bond (Protein Donor)	false
OXT	NZ	LYS- 256	2.89	164.09	H-Bond (Protein Donor)	false
O3P	NZ	LYS- 256	2.84	0	Ionic (Protein Cationic)	false
OXT	NZ	LYS- 256	2.89	0	Ionic (Protein Cationic)	false
O1P	NH2	ARG- 270	2.83	158.82	H-Bond (Protein Donor)	false
O1P	CZ	ARG- 270	3.87	0	Ionic (Protein Cationic)	false
CB	CD	ARG- 270	4.34	0	Hydrophobic	false
C4	CD2	LEU- 320	4.21	0	Hydrophobic	false
C2	CE	MET- 324	4.33	0	Hydrophobic	false
C4	CB	MET- 324	3.92	0	Hydrophobic	false
C5	CB	SER- 325	3.74	0	Hydrophobic	false
C4	CE2	PHE- 330	4.38	0	Hydrophobic	false
C7	CE2	PHE- 330	3.7	0	Hydrophobic	false
C5	CZ	PHE- 330	3.89	0	Hydrophobic	false
C6	CZ	PHE- 361	4.07	0	Hydrophobic	false
S7	CE2	PHE- 361	3.94	0	Hydrophobic	false
CG	CE2	PHE- 362	3.77	0	Hydrophobic	false
C2	CZ	PHE- 362	3.92	0	Hydrophobic	false
C5	CD2	TYR- 367	3.59	0	Hydrophobic	false
C6	CG	TYR- 367	3.85	0	Hydrophobic	false
O2P	N	GLY- 369	2.81	155.2	H-Bond (Protein Donor)	false
CG	CG2	ILE- 380	3.63	0	Hydrophobic	false
CG	CG2	VAL- 381	3.82	0	Hydrophobic	false
S7	CZ	PHE- 443	3.3	0	Hydrophobic	false
S7	CB	ASN- 481	4.05	0	Hydrophobic	false
C7	CG1	VAL- 482	3.99	0	Hydrophobic	false
S7	CG2	VAL- 482	4.11	0	Hydrophobic	false