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Calcium in PDB 8wbr: Crystal Structure of Cis-Epoxysuccinate Hydrolases Klcesh[L]

Protein crystallography data

The structure of Crystal Structure of Cis-Epoxysuccinate Hydrolases Klcesh[L], PDB code: 8wbr was solved by S.Dong, J.S.Xuan, Y.G.Feng, Q.Cui, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.87 / 2.02
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 66.3, 84.749, 92.851, 90, 90, 90
R / Rfree (%) 20.6 / 23.5

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Cis-Epoxysuccinate Hydrolases Klcesh[L] (pdb code 8wbr). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of Cis-Epoxysuccinate Hydrolases Klcesh[L], PDB code: 8wbr:

Calcium binding site 1 out of 1 in 8wbr

Go back to Calcium Binding Sites List in 8wbr
Calcium binding site 1 out of 1 in the Crystal Structure of Cis-Epoxysuccinate Hydrolases Klcesh[L]


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Cis-Epoxysuccinate Hydrolases Klcesh[L] within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca301

b:60.0
occ:1.00
O A:PHE182 2.4 32.0 1.0
O B:HOH335 2.5 41.0 1.0
O A:HOH510 2.6 52.5 1.0
O B:HOH371 2.6 45.1 1.0
O B:PHE182 2.8 30.6 1.0
O A:HOH514 3.4 49.5 1.0
C A:PHE182 3.6 32.6 1.0
C B:PHE182 3.9 28.9 1.0
C A:ASP183 4.1 31.8 1.0
O A:ASP183 4.1 29.3 1.0
CA A:ASP183 4.2 33.7 1.0
N A:ASP183 4.4 25.1 1.0
O B:HOH385 4.4 49.5 1.0
N B:PHE182 4.4 35.8 1.0
N A:PHE182 4.6 33.4 1.0
N A:ALA184 4.6 29.1 1.0
CA A:PHE182 4.6 29.3 1.0
CA B:PHE182 4.6 26.9 1.0
O A:HOH473 4.7 29.1 1.0
C B:ASP183 4.7 30.5 1.0
O B:ASP183 4.8 39.6 1.0
N B:ASP183 4.8 30.6 1.0
CB B:PHE182 4.9 34.1 1.0
CA B:ASP183 4.9 30.0 1.0
N B:ALA184 5.0 25.9 1.0

Reference:

S.Dong, J.Xuan, Y.Feng, Q.Cui. Deciphering the Stereo-Specific Catalytic Mechanisms of Cis-Epoxysuccinate Hydrolases Producing L(+)-Tartaric Acid. J.Biol.Chem. 05635 2024.
ISSN: ESSN 1083-351X
PubMed: 38199576
DOI: 10.1016/J.JBC.2024.105635
Page generated: Thu Jul 10 08:07:30 2025

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