Calcium in PDB 8at8: Structure of Coproporphyrin III-Lmcpfc

Enzymatic activity of Structure of Coproporphyrin III-Lmcpfc

All present enzymatic activity of Structure of Coproporphyrin III-Lmcpfc:
4.99.1.1;

Protein crystallography data

The structure of Structure of Coproporphyrin III-Lmcpfc, PDB code: 8at8 was solved by T.Gabler, S.Hofbauer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.78 / 1.51
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 37.632, 68.069, 63.036, 90, 102.22, 90
R / Rfree (%) 14.6 / 18.2

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of Coproporphyrin III-Lmcpfc (pdb code 8at8). 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 Coproporphyrin III-Lmcpfc, PDB code: 8at8:

Calcium binding site 1 out of 1 in 8at8

Go back to Calcium Binding Sites List in 8at8
Calcium binding site 1 out of 1 in the Structure of Coproporphyrin III-Lmcpfc


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Coproporphyrin III-Lmcpfc within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca407

b:18.6
occ:0.83
O A:HOH586 2.3 20.5 1.0
O2 A:GOL404 2.4 23.9 1.0
O A:HOH558 2.4 23.0 1.0
O3 A:GOL404 2.5 25.4 1.0
O A:HOH625 2.5 21.3 1.0
O A:HOH564 2.5 19.6 1.0
O A:HOH720 2.5 31.0 1.0
O A:HOH518 2.7 25.8 1.0
HO2 A:GOL404 3.0 28.7 1.0
C2 A:GOL404 3.2 45.6 1.0
H2 A:GOL404 3.3 54.7 1.0
C3 A:GOL404 3.4 37.9 1.0
H31 A:GOL404 3.8 45.4 1.0
HA A:SER221 3.9 20.2 1.0
O A:HOH700 4.1 25.7 1.0
H32 A:GOL404 4.2 45.4 1.0
O A:HOH531 4.2 34.6 1.0
O A:GLU222 4.4 19.4 1.0
OD2 A:ASP267 4.4 22.9 1.0
OE2 A:GLU271 4.4 20.1 1.0
OD1 A:ASP267 4.5 21.0 1.0
OE1 A:GLU271 4.5 20.6 1.0
O A:HOH565 4.6 28.1 1.0
C1 A:GOL404 4.7 41.2 1.0
CG A:ASP267 4.8 24.6 1.0
CA A:SER221 4.8 16.9 1.0
H12 A:GOL404 4.8 49.4 1.0
HD3 A:ARG45 4.8 27.5 1.0
CD A:GLU271 4.9 18.6 1.0
HH11 A:ARG45 4.9 30.3 1.0
O A:HOH602 5.0 25.9 1.0
O A:HOH583 5.0 17.4 1.0
NH1 A:ARG45 5.0 25.2 1.0
H A:SER221 5.0 16.1 1.0

Reference:

A.Dali, T.Gabler, F.Sebastiani, A.Destinger, P.G.Furtmuller, V.Pfanzagl, M.Becucci, G.Smulevich, S.Hofbauer. Active Site Architecture of Coproporphyrin Ferrochelatase with Its Physiological Substrate Coproporphyrin III: Propionate Interactions and Porphyrin Core Deformation. Protein Sci. E4534 2022.
ISSN: ESSN 1469-896X
PubMed: 36479958
DOI: 10.1002/PRO.4534
Page generated: Fri Jul 19 07:03:32 2024

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