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Cobalt in PDB 1r6x: The Crystal Structure of A Truncated Form of Yeast Atp Sulfurylase, Lacking the C-Terminal Aps Kinase-Like Domain, in Complex with Sulfate

Enzymatic activity of The Crystal Structure of A Truncated Form of Yeast Atp Sulfurylase, Lacking the C-Terminal Aps Kinase-Like Domain, in Complex with Sulfate

All present enzymatic activity of The Crystal Structure of A Truncated Form of Yeast Atp Sulfurylase, Lacking the C-Terminal Aps Kinase-Like Domain, in Complex with Sulfate:
2.7.7.4;

Protein crystallography data

The structure of The Crystal Structure of A Truncated Form of Yeast Atp Sulfurylase, Lacking the C-Terminal Aps Kinase-Like Domain, in Complex with Sulfate, PDB code: 1r6x was solved by D.J.Lalor, T.Schnyder, V.Saridakis, D.E.Pilloff, A.Dong, H.Tang, T.S.Leyh, E.F.Pai, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.86 / 1.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 50.186, 59.111, 131.165, 90.00, 90.00, 90.00
R / Rfree (%) 19.7 / 21.7

Cobalt Binding Sites:

The binding sites of Cobalt atom in the The Crystal Structure of A Truncated Form of Yeast Atp Sulfurylase, Lacking the C-Terminal Aps Kinase-Like Domain, in Complex with Sulfate (pdb code 1r6x). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the The Crystal Structure of A Truncated Form of Yeast Atp Sulfurylase, Lacking the C-Terminal Aps Kinase-Like Domain, in Complex with Sulfate, PDB code: 1r6x:

Cobalt binding site 1 out of 1 in 1r6x

Go back to Cobalt Binding Sites List in 1r6x
Cobalt binding site 1 out of 1 in the The Crystal Structure of A Truncated Form of Yeast Atp Sulfurylase, Lacking the C-Terminal Aps Kinase-Like Domain, in Complex with Sulfate


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of The Crystal Structure of A Truncated Form of Yeast Atp Sulfurylase, Lacking the C-Terminal Aps Kinase-Like Domain, in Complex with Sulfate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co3000

b:24.3
occ:1.00
 O A:HOH4355 2.1 24.7 1.0
NE2 A:HIS236 2.1 15.2 1.0
O A:HOH4265 2.2 26.7 1.0
NE2 A:HIS235 2.2 19.1 1.0
OD2 A:ASP168 2.7 35.0 1.0
CE1 A:HIS235 3.0 19.8 1.0
CE1 A:HIS236 3.0 15.7 1.0
CD2 A:HIS236 3.1 15.5 1.0
CD2 A:HIS235 3.3 17.2 1.0
CG A:ASP168 3.4 30.9 1.0
OD1 A:ASP168 3.6 31.8 1.0
ND1 A:HIS236 4.1 16.2 1.0
CG A:HIS236 4.1 13.7 1.0
ND1 A:HIS235 4.2 19.3 1.0
O A:HOH4407 4.2 42.7 1.0
O3 A:SO42004 4.3 31.1 1.0
O A:HOH4385 4.3 36.4 1.0
O A:HOH4231 4.3 26.1 1.0
CG A:HIS235 4.4 17.8 1.0
CB A:ASP168 4.5 27.6 1.0

Reference:

D.J.Lalor, T.Schnyder, V.Saridakis, D.E.Pilloff, A.Dong, H.Tang, T.S.Leyh, E.F.Pai. Structural and Functional Analysis of A Truncated Form of Saccharomyces Cerevisiae Atp Sulfurylase: C-Terminal Domain Essential For Oligomer Formation But Not For Activity Protein Eng. V. 16 1071 2003.
ISSN: ISSN 0269-2139
PubMed: 14983089
DOI: 10.1093/PROTEIN/GZG133
Page generated: Tue Jul 30 14:33:57 2024

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