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Calcium in PDB 1zm1: Crystal Structures of Complex F. Succinogenes 1,3-1,4-Beta- D-Glucanase and Beta-1,3-1,4-Cellotriose

Enzymatic activity of Crystal Structures of Complex F. Succinogenes 1,3-1,4-Beta- D-Glucanase and Beta-1,3-1,4-Cellotriose

All present enzymatic activity of Crystal Structures of Complex F. Succinogenes 1,3-1,4-Beta- D-Glucanase and Beta-1,3-1,4-Cellotriose:
3.2.1.73;

Protein crystallography data

The structure of Crystal Structures of Complex F. Succinogenes 1,3-1,4-Beta- D-Glucanase and Beta-1,3-1,4-Cellotriose, PDB code: 1zm1 was solved by L.C.Tsai, L.F.Shyur, Y.S.Cheng, S.H.Lee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 2.30
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 70.148, 43.970, 81.015, 90.00, 109.56, 90.00
R / Rfree (%) 18 / 26.4

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structures of Complex F. Succinogenes 1,3-1,4-Beta- D-Glucanase and Beta-1,3-1,4-Cellotriose (pdb code 1zm1). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structures of Complex F. Succinogenes 1,3-1,4-Beta- D-Glucanase and Beta-1,3-1,4-Cellotriose, PDB code: 1zm1:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1zm1

Go back to Calcium Binding Sites List in 1zm1
Calcium binding site 1 out of 2 in the Crystal Structures of Complex F. Succinogenes 1,3-1,4-Beta- D-Glucanase and Beta-1,3-1,4-Cellotriose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structures of Complex F. Succinogenes 1,3-1,4-Beta- D-Glucanase and Beta-1,3-1,4-Cellotriose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca400

b:30.3
occ:1.00
O A:GLY222 2.3 34.6 1.0
O A:ASN189 2.4 26.4 1.0
O A:ASN164 2.4 24.4 1.0
OD1 A:ASN164 2.5 25.4 1.0
O A:HOH458 2.7 23.3 1.0
O A:HOH459 2.7 25.4 1.0
O A:HOH520 2.8 22.4 1.0
CG A:ASN164 3.4 23.7 1.0
C A:ASN164 3.4 22.9 1.0
C A:ASN189 3.4 26.9 1.0
C A:GLY222 3.4 34.0 1.0
CA A:ASN164 3.9 23.5 1.0
CA A:ASN189 4.0 26.5 1.0
CA A:GLY222 4.0 34.3 1.0
CB A:ASN189 4.2 25.7 1.0
ND2 A:ASN164 4.2 24.7 1.0
CB A:ASN164 4.3 25.1 1.0
CG A:MSE223 4.5 40.3 1.0
N A:TRP165 4.5 23.1 1.0
N A:MSE223 4.5 34.1 1.0
N A:PHE190 4.5 27.4 1.0
O A:HOH519 4.7 41.2 1.0
CB A:TRP165 4.7 23.5 1.0
CA A:MSE223 4.8 35.3 1.0
CB A:PHE190 4.8 28.6 1.0
O A:PHE190 4.9 30.1 1.0
CA A:TRP165 4.9 21.9 1.0
C A:PHE190 4.9 30.4 1.0
OD1 A:ASN189 4.9 24.4 1.0
OD1 A:ASP191 4.9 33.7 1.0
CA A:PHE190 5.0 29.4 1.0

Calcium binding site 2 out of 2 in 1zm1

Go back to Calcium Binding Sites List in 1zm1
Calcium binding site 2 out of 2 in the Crystal Structures of Complex F. Succinogenes 1,3-1,4-Beta- D-Glucanase and Beta-1,3-1,4-Cellotriose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structures of Complex F. Succinogenes 1,3-1,4-Beta- D-Glucanase and Beta-1,3-1,4-Cellotriose within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca1400

b:42.2
occ:1.00
O B:GLY222 2.4 36.3 1.0
OD1 B:ASN164 2.4 28.2 1.0
O B:ASN189 2.5 33.5 1.0
O B:ASN164 2.6 26.6 1.0
O B:HOH1426 2.8 27.5 1.0
O B:HOH1557 2.8 29.4 1.0
C B:GLY222 3.4 36.8 1.0
C B:ASN189 3.5 32.9 1.0
C B:ASN164 3.5 27.7 1.0
CG B:ASN164 3.6 28.8 1.0
CB B:ASN189 3.9 32.4 1.0
CA B:ASN189 3.9 33.4 1.0
CA B:GLY222 4.0 37.7 1.0
CA B:ASN164 4.0 27.2 1.0
OD1 B:ASN189 4.3 30.0 1.0
CB B:ASN164 4.4 28.1 1.0
N B:MSE223 4.5 36.9 1.0
OD1 B:ASP191 4.5 37.9 1.0
N B:TRP165 4.5 28.3 1.0
CG B:ASN189 4.6 32.1 1.0
ND2 B:ASN164 4.6 30.4 1.0
CB B:TRP165 4.7 27.9 1.0
N B:PHE190 4.7 33.2 1.0
CA B:MSE223 4.8 35.2 1.0
CA B:TRP165 4.9 28.6 1.0

Reference:

L.C.Tsai, L.F.Shyur, Y.S.Cheng, S.H.Lee. Crystal Structure of Truncated Fibrobacter Succinogenes 1,3-1,4-Beta-D-Glucanase in Complex with Beta-1,3-1,4-Cellotriose J.Mol.Biol. V. 354 642 2005.
ISSN: ISSN 0022-2836
PubMed: 16246371
DOI: 10.1016/J.JMB.2005.09.041
Page generated: Tue Jul 8 04:05:29 2025

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