Chlorine in PDB 3sqg: Crystal Structure of A Methyl-Coenzyme M Reductase Purified From Black Sea Mats

Enzymatic activity of Crystal Structure of A Methyl-Coenzyme M Reductase Purified From Black Sea Mats

All present enzymatic activity of Crystal Structure of A Methyl-Coenzyme M Reductase Purified From Black Sea Mats:
2.8.4.1;

Protein crystallography data

The structure of Crystal Structure of A Methyl-Coenzyme M Reductase Purified From Black Sea Mats, PDB code: 3sqg was solved by S.Shima, M.Krueger, T.Weinert, U.Demmer, R.K.Thauer, U.Ermler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	47.58 / 2.10
*Space group*	C 2 2 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	128.860, 412.490, 165.510, 90.00, 90.00, 90.00
*R / R_free (%)*	16.1 / 20.6

Other elements in 3sqg:

The structure of Crystal Structure of A Methyl-Coenzyme M Reductase Purified From Black Sea Mats also contains other interesting chemical elements:

Nickel	(Ni)	3 atoms
Calcium	(Ca)	2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of A Methyl-Coenzyme M Reductase Purified From Black Sea Mats (pdb code 3sqg). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of A Methyl-Coenzyme M Reductase Purified From Black Sea Mats, PDB code: 3sqg:

Chlorine binding site 1 out of 1 in 3sqg

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Chlorine Binding Sites List in 3sqg

Chlorine binding site 1 out of 1 in the Crystal Structure of A Methyl-Coenzyme M Reductase Purified From Black Sea Mats

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of A Methyl-Coenzyme M Reductase Purified From Black Sea Mats within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl586 b:47.5 occ:1.00	OH	A:TYR253	2.6	34.0	1.0
	CE1	A:HIS121	2.9	29.2	1.0
	CZ	A:TYR253	3.4	35.5	1.0
	CE1	A:TYR253	3.4	31.8	1.0
	CG	A:TYR140	3.5	26.7	1.0
	CB	A:TYR140	3.6	24.9	1.0
	CD2	A:TYR140	3.8	28.9	1.0
	CG1	A:ILE137	3.8	28.3	1.0
	ND1	A:HIS121	3.8	30.9	1.0
	NE2	A:HIS121	3.9	29.0	1.0
	CA	A:ILE137	3.9	28.3	1.0
	CD1	A:TYR140	4.0	26.6	1.0
	CD1	A:LEU117	4.3	34.5	1.0
	O	A:THR136	4.3	26.6	1.0
	CB	A:ILE137	4.3	28.5	1.0
	CD2	A:LEU117	4.4	32.3	1.0
	CE2	A:TYR140	4.4	30.3	1.0
	N	A:ILE137	4.5	26.8	1.0
	CE1	A:TYR140	4.6	29.1	1.0
	CE	A:MET249	4.6	76.0	1.0
	CG2	A:ILE137	4.7	25.9	1.0
	C	A:THR136	4.7	26.9	1.0
	CE2	A:TYR253	4.7	36.5	1.0
	CD1	A:TYR253	4.8	30.5	1.0
	CZ	A:TYR140	4.8	31.5	1.0
	O	A:ILE137	4.9	27.4	1.0
	CG1	A:VAL132	4.9	33.0	1.0
	C	A:ILE137	4.9	28.6	1.0
	CG	A:LEU117	5.0	34.0	1.0

Reference:

S.Shima, M.Krueger, T.Weinert, U.Demmer, J.Kahnt, R.K.Thauer, U.Ermler. Structure of A Methyl-Coenzyme M Reductase From Black Sea Mats That Oxidize Methane Anaerobically. Nature V. 481 98 2011.
ISSN: ISSN 0028-0836
PubMed: 22121022
DOI: 10.1038/NATURE10663

Page generated: Sun Jul 21 04:43:51 2024

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