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Magnesium in PDB 3q6j: Structural Basis For Carbon Dioxide Binding By 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase

Enzymatic activity of Structural Basis For Carbon Dioxide Binding By 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase

All present enzymatic activity of Structural Basis For Carbon Dioxide Binding By 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase:
1.8.1.5;

Protein crystallography data

The structure of Structural Basis For Carbon Dioxide Binding By 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase, PDB code: 3q6j was solved by A.S.Pandey, D.W.Mulder, S.A.Ensign, J.W.Peters, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.92
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 88.466, 59.803, 105.463, 90.00, 102.28, 90.00
R / Rfree (%) 16.4 / 22.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structural Basis For Carbon Dioxide Binding By 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase (pdb code 3q6j). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structural Basis For Carbon Dioxide Binding By 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase, PDB code: 3q6j:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3q6j

Go back to Magnesium Binding Sites List in 3q6j
Magnesium binding site 1 out of 2 in the Structural Basis For Carbon Dioxide Binding By 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structural Basis For Carbon Dioxide Binding By 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg527

b:22.4
occ:1.00
OG A:SER450 2.3 15.5 1.0
O A:ALA447 2.3 16.9 1.0
O A:LEU431 2.4 17.7 1.0
O A:VAL429 2.4 16.2 1.0
O A:HOH686 2.4 18.8 1.0
O A:LEU427 3.1 24.7 1.0
C A:LEU431 3.3 17.8 1.0
C A:ALA447 3.4 22.7 1.0
CB A:SER450 3.4 15.8 1.0
C A:VAL429 3.6 18.5 1.0
N A:LEU431 3.8 19.8 1.0
N A:SER450 4.1 17.6 1.0
N A:PRO432 4.2 22.7 1.0
CA A:LEU431 4.2 21.1 1.0
CA A:HIS448 4.2 20.1 1.0
CA A:SER450 4.2 20.3 1.0
N A:HIS448 4.2 19.1 1.0
N A:VAL429 4.3 22.3 1.0
CD A:PRO432 4.3 16.4 1.0
C A:LEU427 4.3 26.3 1.0
CA A:ALA447 4.4 15.2 1.0
C A:HIS448 4.4 23.4 1.0
C A:ALA430 4.4 22.4 1.0
CB A:ALA447 4.5 13.9 1.0
O A:PRO432 4.5 16.2 1.0
N A:ALA430 4.5 17.9 1.0
CG A:PRO420 4.6 24.4 1.0
CA A:VAL429 4.6 16.8 1.0
CG2 A:VAL429 4.6 18.1 1.0
CA A:ALA430 4.6 21.8 1.0
O A:HIS448 4.6 16.3 1.0
C A:SER450 4.7 17.2 1.0
O A:GLY451 4.7 16.8 1.0
N A:GLY451 4.8 17.0 1.0
CB A:PRO420 4.8 21.6 1.0
N A:MET449 4.9 16.6 1.0

Magnesium binding site 2 out of 2 in 3q6j

Go back to Magnesium Binding Sites List in 3q6j
Magnesium binding site 2 out of 2 in the Structural Basis For Carbon Dioxide Binding By 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structural Basis For Carbon Dioxide Binding By 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg527

b:22.8
occ:1.00
O B:HOH574 2.4 16.1 1.0
OG B:SER450 2.4 11.0 1.0
O B:ALA447 2.4 12.3 1.0
O B:VAL429 2.5 13.5 1.0
O B:LEU431 2.5 19.5 1.0
O B:LEU427 3.2 16.2 1.0
C B:LEU431 3.4 16.8 1.0
C B:ALA447 3.5 14.1 1.0
CB B:SER450 3.6 12.5 1.0
C B:VAL429 3.7 15.2 1.0
N B:LEU431 4.0 16.2 1.0
N B:SER450 4.1 11.7 1.0
CA B:HIS448 4.1 13.6 1.0
N B:PRO432 4.2 19.4 1.0
N B:HIS448 4.2 17.2 1.0
CD B:PRO432 4.2 14.7 1.0
N B:VAL429 4.3 17.3 1.0
CA B:LEU431 4.3 15.4 1.0
CG B:PRO420 4.3 23.8 1.0
C B:LEU427 4.3 17.6 1.0
CA B:SER450 4.3 12.9 1.0
C B:HIS448 4.4 20.6 1.0
C B:ALA430 4.4 21.0 1.0
CA B:ALA447 4.4 13.6 1.0
CG2 B:VAL429 4.5 16.5 1.0
CB B:ALA447 4.6 14.0 1.0
N B:ALA430 4.6 16.7 1.0
O B:PRO432 4.6 16.1 1.0
CA B:VAL429 4.6 15.7 1.0
CA B:ALA430 4.6 19.1 1.0
O B:HIS448 4.7 15.8 1.0
O B:GLY451 4.7 12.3 1.0
C B:SER450 4.8 12.0 1.0
N B:GLY451 4.8 16.9 1.0
N B:MET449 5.0 18.1 1.0

Reference:

A.S.Pandey, D.W.Mulder, S.A.Ensign, J.W.Peters. Structural Basis For Carbon Dioxide Binding By 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase. Febs Lett. V. 585 459 2011.
ISSN: ISSN 0014-5793
PubMed: 21192936
DOI: 10.1016/J.FEBSLET.2010.12.035
Page generated: Thu Aug 15 09:57:36 2024

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