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Calcium in PDB 6qz3: Structure of Mhetase From Ideonella Sakaiensis

Enzymatic activity of Structure of Mhetase From Ideonella Sakaiensis

All present enzymatic activity of Structure of Mhetase From Ideonella Sakaiensis:
3.1.1.102;

Protein crystallography data

The structure of Structure of Mhetase From Ideonella Sakaiensis, PDB code: 6qz3 was solved by M.D.Allen, C.W.Johnson, B.C.Knott, G.T.Beckham, J.E.Mcgeehan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.82 / 1.60
Space group P 2 21 21
Cell size a, b, c (Å), α, β, γ (°) 77.368, 89.016, 91.643, 90.00, 90.00, 90.00
R / Rfree (%) 16.2 / 17.8

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of Mhetase From Ideonella Sakaiensis (pdb code 6qz3). 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 Structure of Mhetase From Ideonella Sakaiensis, PDB code: 6qz3:

Calcium binding site 1 out of 1 in 6qz3

Go back to Calcium Binding Sites List in 6qz3
Calcium binding site 1 out of 1 in the Structure of Mhetase From Ideonella Sakaiensis


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Mhetase From Ideonella Sakaiensis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca702

b:20.2
occ:1.00
O A:LEU309 2.3 19.8 1.0
O A:ILE313 2.4 18.4 1.0
OD1 A:ASP304 2.5 20.5 1.0
OD2 A:ASP307 2.5 22.8 1.0
O A:ASP304 2.5 20.4 1.0
OD1 A:ASP311 2.5 19.0 1.0
O A:HOH823 2.5 22.7 1.0
OD1 A:ASP307 2.7 22.6 1.0
CG A:ASP307 2.9 21.8 1.0
C A:ASP304 3.5 20.0 1.0
CG A:ASP311 3.5 22.6 1.0
C A:LEU309 3.6 21.6 1.0
C A:ILE313 3.6 18.6 1.0
CG A:ASP304 3.7 21.6 1.0
OD2 A:ASP311 4.0 24.2 1.0
N A:ASP311 4.0 21.0 1.0
CA A:ASP304 4.0 23.2 1.0
N A:ILE313 4.2 17.5 1.0
OD2 A:ASP315 4.3 33.6 1.0
CA A:ILE313 4.4 17.7 1.0
CB A:ASP307 4.4 22.1 1.0
CA A:LEU309 4.5 20.3 1.0
CB A:ASP304 4.5 23.8 1.0
O A:HOH945 4.5 19.6 1.0
N A:ALA310 4.5 20.7 1.0
CA A:ALA310 4.5 17.5 1.0
N A:LEU309 4.5 20.1 1.0
N A:ALA305 4.5 22.3 1.0
N A:VAL314 4.6 16.0 1.0
OD2 A:ASP304 4.6 23.4 1.0
N A:ASP315 4.6 18.3 1.0
CB A:LEU309 4.7 23.6 1.0
CB A:ASP311 4.7 17.8 1.0
C A:ALA310 4.7 21.6 1.0
CB A:ILE313 4.7 17.0 1.0
CA A:VAL314 4.7 19.6 1.0
CA A:ALA305 4.8 24.1 1.0
CA A:ASP311 4.8 21.5 1.0
O A:HOH1228 4.9 30.8 1.0
N A:GLY312 5.0 19.2 1.0

Reference:

B.C.Knott, E.Erickson, M.D.Allen, J.E.Gado, R.Graham, F.L.Kearns, I.Pardo, E.Topuzlu, J.J.Anderson, H.P.Austin, G.Dominick, C.W.Johnson, N.A.Rorrer, C.J.Szostkiewicz, V.Copie, C.M.Payne, H.L.Woodcock, B.S.Donohoe, G.T.Beckham, J.E.Mcgeehan. Characterization and Engineering of A Two-Enzyme System For Plastics Depolymerization. Proc.Natl.Acad.Sci.Usa V. 117 25476 2020.
ISSN: ESSN 1091-6490
PubMed: 32989159
DOI: 10.1073/PNAS.2006753117
Page generated: Tue Jul 16 14:09:22 2024

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