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Magnesium in PDB 2ywr: Crystal Structure of Gar Transformylase From Aquifex Aeolicus

Enzymatic activity of Crystal Structure of Gar Transformylase From Aquifex Aeolicus

All present enzymatic activity of Crystal Structure of Gar Transformylase From Aquifex Aeolicus:
2.1.2.2;

Protein crystallography data

The structure of Crystal Structure of Gar Transformylase From Aquifex Aeolicus, PDB code: 2ywr was solved by M.Kanagawa, S.Baba, S.Kuramitsu, S.Yokoyama, G.Kawai, G.Sampei, Rikenstructural Genomics/Proteomics Initiative (Rsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.40 / 1.77
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 59.955, 59.955, 105.934, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 21.9

Other elements in 2ywr:

The structure of Crystal Structure of Gar Transformylase From Aquifex Aeolicus also contains other interesting chemical elements:

Cobalt (Co) 4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Gar Transformylase From Aquifex Aeolicus (pdb code 2ywr). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Gar Transformylase From Aquifex Aeolicus, PDB code: 2ywr:

Magnesium binding site 1 out of 1 in 2ywr

Go back to Magnesium Binding Sites List in 2ywr
Magnesium binding site 1 out of 1 in the Crystal Structure of Gar Transformylase From Aquifex Aeolicus


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Gar Transformylase From Aquifex Aeolicus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg703

b:14.3
occ:1.00
O A:HOH911 2.8 32.7 1.0
O A:HOH899 3.2 29.6 1.0
O A:HOH992 3.2 44.0 1.0
ND2 A:ASN14 3.2 11.5 1.0
O A:HOH784 3.3 15.7 1.0
N A:ASN14 3.4 12.8 1.0
CB A:ASN14 3.4 11.9 1.0
N A:SER13 3.7 15.9 1.0
CG A:ASN14 3.8 11.4 1.0
C A:ALA87 3.8 16.7 1.0
O A:ALA87 3.8 15.4 1.0
CA A:GLY12 3.9 18.6 1.0
N A:GLY88 3.9 16.3 1.0
CA A:ASN14 4.0 12.6 1.0
C A:GLY12 4.0 17.8 1.0
CA A:GLY88 4.0 17.2 1.0
OG A:SER13 4.1 15.6 1.0
N A:GLY12 4.2 19.7 1.0
C A:SER13 4.4 14.9 1.0
CB A:ALA87 4.5 16.3 1.0
CA A:ALA87 4.5 15.3 1.0
O A:HOH777 4.5 14.4 1.0
CA A:SER13 4.5 15.7 1.0
N A:LEU15 4.8 12.5 1.0
O A:GLY12 4.9 16.4 1.0
CB A:SER13 4.9 17.6 1.0
C A:ASN14 4.9 13.0 1.0

Reference:

G.Sampei, M.Kanagawa, S.Baba, T.Shimasaki, H.Taka, S.Mitsui, S.Fujiwara, Y.Yanagida, M.Kusano, S.Suzuki, K.Terao, H.Kawai, Y.Fukai, N.Nakagawa, A.Ebihara, S.Kuramitsu, S.Yokoyama, G.Kawai. Structures and Reaction Mechanisms of the Two Related Enzymes, Purn and Puru. J.Biochem. V. 154 569 2013.
ISSN: ISSN 0021-924X
PubMed: 24108189
DOI: 10.1093/JB/MVT090
Page generated: Wed Aug 14 07:41:18 2024

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