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Zinc in PDB 2qha: From Structure to Function: Insights Into the Catalytic Substrate Specificity and Thermostability Displayed By Bacillus Subtilis Mannanase Bcman

Enzymatic activity of From Structure to Function: Insights Into the Catalytic Substrate Specificity and Thermostability Displayed By Bacillus Subtilis Mannanase Bcman

All present enzymatic activity of From Structure to Function: Insights Into the Catalytic Substrate Specificity and Thermostability Displayed By Bacillus Subtilis Mannanase Bcman:
3.2.1.78;

Protein crystallography data

The structure of From Structure to Function: Insights Into the Catalytic Substrate Specificity and Thermostability Displayed By Bacillus Subtilis Mannanase Bcman, PDB code: 2qha was solved by X.X.Yan, D.C.Liang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.45
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 45.179, 58.785, 63.463, 83.03, 82.42, 77.61
R / Rfree (%) 15.8 / 19

Zinc Binding Sites:

The binding sites of Zinc atom in the From Structure to Function: Insights Into the Catalytic Substrate Specificity and Thermostability Displayed By Bacillus Subtilis Mannanase Bcman (pdb code 2qha). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the From Structure to Function: Insights Into the Catalytic Substrate Specificity and Thermostability Displayed By Bacillus Subtilis Mannanase Bcman, PDB code: 2qha:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2qha

Go back to Zinc Binding Sites List in 2qha
Zinc binding site 1 out of 2 in the From Structure to Function: Insights Into the Catalytic Substrate Specificity and Thermostability Displayed By Bacillus Subtilis Mannanase Bcman


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of From Structure to Function: Insights Into the Catalytic Substrate Specificity and Thermostability Displayed By Bacillus Subtilis Mannanase Bcman within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn2001

b:9.5
occ:0.43
NE2 A:HIS23 2.1 10.6 1.0
OE1 A:GLU336 2.1 14.8 1.0
ND1 A:HIS1 2.1 17.5 1.0
O A:HIS1 2.1 15.8 1.0
N A:HIS1 2.2 16.2 1.0
OE2 A:GLU336 2.3 15.3 1.0
CD A:GLU336 2.5 15.5 1.0
C A:HIS1 2.8 16.0 1.0
CA A:HIS1 2.9 16.3 1.0
CE1 A:HIS23 3.0 10.0 1.0
CE1 A:HIS1 3.1 17.2 1.0
CD2 A:HIS23 3.1 10.1 1.0
CG A:HIS1 3.1 16.8 1.0
O A:HOH2467 3.5 38.1 1.0
CB A:HIS1 3.5 16.3 1.0
O A:HOH2121 3.9 23.1 1.0
CG A:GLU336 4.1 16.0 1.0
N A:THR2 4.1 15.5 1.0
ND1 A:HIS23 4.1 9.7 1.0
NE2 A:HIS1 4.2 17.7 1.0
CG A:HIS23 4.2 9.7 1.0
CD2 A:HIS1 4.2 17.8 1.0
O A:HOH2322 4.5 31.9 1.0
O A:HOH2344 4.7 33.5 1.0
O A:HOH2240 4.8 25.3 1.0
CB A:GLU336 4.8 16.3 1.0
CA A:THR2 4.8 15.7 1.0
O A:HOH2320 4.9 35.6 1.0

Zinc binding site 2 out of 2 in 2qha

Go back to Zinc Binding Sites List in 2qha
Zinc binding site 2 out of 2 in the From Structure to Function: Insights Into the Catalytic Substrate Specificity and Thermostability Displayed By Bacillus Subtilis Mannanase Bcman


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of From Structure to Function: Insights Into the Catalytic Substrate Specificity and Thermostability Displayed By Bacillus Subtilis Mannanase Bcman within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn2002

b:10.9
occ:0.40
NE2 B:HIS23 2.1 12.9 1.0
ND1 B:HIS1 2.1 18.9 1.0
O B:HIS1 2.1 16.4 1.0
OE2 B:GLU336 2.1 17.3 1.0
N B:HIS1 2.2 17.6 1.0
OE1 B:GLU336 2.2 18.8 1.0
CD B:GLU336 2.5 18.2 1.0
C B:HIS1 2.8 17.2 1.0
CA B:HIS1 2.9 17.4 1.0
CE1 B:HIS23 3.0 12.3 1.0
CE1 B:HIS1 3.0 18.7 1.0
CG B:HIS1 3.1 18.5 1.0
CD2 B:HIS23 3.1 12.4 1.0
CB B:HIS1 3.5 18.1 1.0
CG B:GLU336 4.0 18.6 1.0
O B:HOH2135 4.0 18.7 1.0
N B:THR2 4.1 17.0 1.0
ND1 B:HIS23 4.1 11.3 1.0
NE2 B:HIS1 4.2 19.6 1.0
CD2 B:HIS1 4.2 19.2 1.0
CG B:HIS23 4.2 10.9 1.0
O B:HOH2200 4.3 23.6 1.0
CB B:GLU336 4.8 19.0 1.0
CA B:THR2 4.9 16.8 1.0

Reference:

X.X.Yan, X.M.An, L.L.Gui, D.C.Liang. From Structure to Function: Insights Into the Catalytic Substrate Specificity and Thermostability Displayed By Bacillus Subtilis Mannanase Bcman J.Mol.Biol. V. 379 535 2008.
ISSN: ISSN 0022-2836
PubMed: 18455734
DOI: 10.1016/J.JMB.2008.03.068
Page generated: Wed Dec 16 03:50:26 2020

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