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Calcium in PDB 6h6x: Structure of An Evolved Dimeric Form of the Ubid-Class Enzyme Hmff From Pelotomaculum Thermopropionicum in Complex with Prfmn

Protein crystallography data

The structure of Structure of An Evolved Dimeric Form of the Ubid-Class Enzyme Hmff From Pelotomaculum Thermopropionicum in Complex with Prfmn, PDB code: 6h6x was solved by K.A.P.Payne, D.Leys, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 83.86 / 2.25
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 167.720, 63.930, 98.300, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 24.8

Other elements in 6h6x:

The structure of Structure of An Evolved Dimeric Form of the Ubid-Class Enzyme Hmff From Pelotomaculum Thermopropionicum in Complex with Prfmn also contains other interesting chemical elements:

Potassium (K) 2 atoms
Manganese (Mn) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of An Evolved Dimeric Form of the Ubid-Class Enzyme Hmff From Pelotomaculum Thermopropionicum in Complex with Prfmn (pdb code 6h6x). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structure of An Evolved Dimeric Form of the Ubid-Class Enzyme Hmff From Pelotomaculum Thermopropionicum in Complex with Prfmn, PDB code: 6h6x:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 6h6x

Go back to Calcium Binding Sites List in 6h6x
Calcium binding site 1 out of 2 in the Structure of An Evolved Dimeric Form of the Ubid-Class Enzyme Hmff From Pelotomaculum Thermopropionicum in Complex with Prfmn


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of An Evolved Dimeric Form of the Ubid-Class Enzyme Hmff From Pelotomaculum Thermopropionicum in Complex with Prfmn within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca504

b:45.1
occ:1.00
O B:ARG385 2.6 35.6 1.0
O B:THR420 2.7 37.9 1.0
OD2 B:ASP391 2.8 46.2 1.0
O B:ASP418 2.9 31.6 1.0
O B:HOH696 2.9 54.3 1.0
CG B:ASP391 3.2 45.9 1.0
OD1 B:ASP391 3.4 52.1 1.0
NH2 B:ARG390 3.4 71.5 1.0
C B:ASP418 3.7 32.2 1.0
OD1 B:ASP418 3.7 42.6 1.0
N B:THR420 3.8 36.9 1.0
C B:ARG385 3.8 39.7 1.0
C B:THR420 3.8 37.2 1.0
CG B:ASP418 3.8 46.6 1.0
CA B:ALA419 4.1 31.6 1.0
C B:ALA419 4.2 33.1 1.0
OD2 B:ASP418 4.2 46.7 1.0
CB B:ASP391 4.2 41.8 1.0
N B:ALA419 4.3 31.0 1.0
CB B:ASP418 4.3 40.9 1.0
CA B:THR420 4.4 39.8 1.0
CA B:CYS386 4.4 39.2 1.0
CZ B:ARG390 4.5 74.5 1.0
N B:CYS386 4.5 40.5 1.0
OG1 B:THR420 4.6 36.8 1.0
CA B:ASP418 4.7 35.8 1.0
NE B:ARG390 4.7 68.6 1.0
CG B:PRO422 4.7 62.4 1.0
CB B:ARG385 4.8 30.1 1.0
CD B:PRO422 4.8 59.3 1.0
CA B:ARG385 4.8 35.3 1.0
N B:ILE421 5.0 41.1 1.0
N B:GLN387 5.0 40.6 1.0

Calcium binding site 2 out of 2 in 6h6x

Go back to Calcium Binding Sites List in 6h6x
Calcium binding site 2 out of 2 in the Structure of An Evolved Dimeric Form of the Ubid-Class Enzyme Hmff From Pelotomaculum Thermopropionicum in Complex with Prfmn


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of An Evolved Dimeric Form of the Ubid-Class Enzyme Hmff From Pelotomaculum Thermopropionicum in Complex with Prfmn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca504

b:44.1
occ:1.00
O A:ARG385 2.6 40.3 1.0
O A:HOH656 2.7 53.7 1.0
O A:THR420 2.7 42.4 1.0
OD2 A:ASP391 2.8 39.5 1.0
O A:ASP418 2.9 36.7 1.0
CG A:ASP391 3.3 44.2 1.0
NH2 A:ARG390 3.4 67.4 1.0
OD1 A:ASP391 3.5 52.6 1.0
N A:THR420 3.7 35.0 1.0
C A:ASP418 3.7 33.0 1.0
OD1 A:ASP418 3.7 34.9 1.0
C A:THR420 3.8 43.4 1.0
C A:ARG385 3.8 37.1 1.0
CG A:ASP418 3.9 38.2 1.0
CA A:ALA419 4.1 34.5 1.0
C A:ALA419 4.1 38.1 1.0
CB A:ASP391 4.3 41.5 1.0
N A:ALA419 4.3 33.9 1.0
CB A:ASP418 4.3 38.1 1.0
CA A:THR420 4.3 40.5 1.0
OD2 A:ASP418 4.3 42.8 1.0
CA A:CYS386 4.4 38.3 1.0
CZ A:ARG390 4.5 70.7 1.0
OG1 A:THR420 4.5 37.5 1.0
N A:CYS386 4.6 41.0 1.0
NE A:ARG390 4.7 70.6 1.0
CA A:ASP418 4.7 33.6 1.0
CB A:ARG385 4.8 37.4 1.0
CD A:PRO422 4.8 60.7 1.0
CG A:PRO422 4.8 59.0 1.0
CA A:ARG385 4.8 35.2 1.0
N A:ILE421 4.9 44.9 1.0
N A:GLN387 5.0 39.8 1.0

Reference:

K.A.P.Payne, S.A.Marshall, K.Fisher, M.J.Cliff, D.M.Cannas, C.Yan, D.J.Heyes, D.A.Parker, I.Larrosa, D.Leys. Enzymatic Carboxylation of 2-Furoic Acid Yields 2,5-Furandicarboxylic Acid (Fdca). Acs Catalysis V. 9 2854 2019.
ISSN: ESSN 2155-5435
PubMed: 31057985
DOI: 10.1021/ACSCATAL.8B04862
Page generated: Wed Jul 9 14:32:21 2025

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