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Calcium in PDB 7lst: Ruminococcus Bromii AMY12-D392A with 63-A-D-Glucosyl-Maltotriosyl- Maltotriose

Enzymatic activity of Ruminococcus Bromii AMY12-D392A with 63-A-D-Glucosyl-Maltotriosyl- Maltotriose

All present enzymatic activity of Ruminococcus Bromii AMY12-D392A with 63-A-D-Glucosyl-Maltotriosyl- Maltotriose:
3.2.1.41;

Protein crystallography data

The structure of Ruminococcus Bromii AMY12-D392A with 63-A-D-Glucosyl-Maltotriosyl- Maltotriose, PDB code: 7lst was solved by N.M.Koropatkin, D.W.Cockburn, H.A.Brown, R.D.Kibler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 85.26 / 2.05
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.981, 99.107, 167.236, 90, 90, 90
R / Rfree (%) 18 / 23.2

Other elements in 7lst:

The structure of Ruminococcus Bromii AMY12-D392A with 63-A-D-Glucosyl-Maltotriosyl- Maltotriose also contains other interesting chemical elements:

Sodium (Na) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Ruminococcus Bromii AMY12-D392A with 63-A-D-Glucosyl-Maltotriosyl- Maltotriose (pdb code 7lst). 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 Ruminococcus Bromii AMY12-D392A with 63-A-D-Glucosyl-Maltotriosyl- Maltotriose, PDB code: 7lst:

Calcium binding site 1 out of 1 in 7lst

Go back to Calcium Binding Sites List in 7lst
Calcium binding site 1 out of 1 in the Ruminococcus Bromii AMY12-D392A with 63-A-D-Glucosyl-Maltotriosyl- Maltotriose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Ruminococcus Bromii AMY12-D392A with 63-A-D-Glucosyl-Maltotriosyl- Maltotriose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca920

b:22.5
occ:1.00
OE2 A:GLU268 2.2 23.9 1.0
O A:PHE263 2.3 22.4 1.0
OD1 A:ASP262 2.4 24.0 1.0
O A:HOH1023 2.4 18.7 1.0
O A:HOH1035 2.5 21.1 1.0
O A:HOH1263 2.6 17.8 1.0
OE1 A:GLU288 2.6 21.7 1.0
CD A:GLU268 3.3 25.2 1.0
CD A:GLU288 3.4 21.9 1.0
CG A:ASP262 3.4 24.2 1.0
OE2 A:GLU288 3.5 22.4 1.0
C A:PHE263 3.5 22.4 1.0
N A:PHE263 3.7 21.8 1.0
O A:HOH1295 3.8 22.2 1.0
CG A:GLU268 3.9 25.3 1.0
OD2 A:ASP262 4.0 25.1 1.0
O A:VAL266 4.2 24.5 1.0
CA A:PHE263 4.2 21.6 1.0
OE1 A:GLU268 4.3 25.8 1.0
C A:ASP262 4.4 22.1 1.0
N A:GLN264 4.5 22.7 1.0
N A:GLY289 4.5 22.6 1.0
CA A:ASP262 4.6 22.5 1.0
CB A:ASP262 4.6 23.4 1.0
CA A:GLN264 4.8 23.5 1.0
CG A:GLU288 4.8 21.5 1.0
OD1 A:ASN167 4.8 26.1 1.0
O A:HOH1094 4.8 28.3 1.0
CD1 A:PHE263 4.8 21.0 1.0
CA A:ASN167 4.9 25.6 1.0
C A:GLN264 5.0 23.5 1.0

Reference:

D.W.Cockburn, R.Kibler, H.A.Brown, R.Duvall, S.Morais, E.Bayer, N.M.Koropatkin. Structure and Substrate Recognition By the Ruminococcus Bromii Amylosome Pullulanases. J.Struct.Biol. V. 213 07765 2021.
ISSN: ESSN 1095-8657
PubMed: 34186214
DOI: 10.1016/J.JSB.2021.107765
Page generated: Fri Jul 19 01:46:51 2024

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