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Zinc in PDB 1bao: The Contribution of Buried Hydrogen Bonds to Protein Stability: the Crystal Structures of Two Barnase Mutants

Protein crystallography data

The structure of The Contribution of Buried Hydrogen Bonds to Protein Stability: the Crystal Structures of Two Barnase Mutants, PDB code: 1bao was solved by Y.W.Chen, A.R.Fersht, K.Henrick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 2.20
Space group P 32
Cell size a, b, c (Å), α, β, γ (°) 58.809, 58.809, 81.902, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Zinc Binding Sites:

The binding sites of Zinc atom in the The Contribution of Buried Hydrogen Bonds to Protein Stability: the Crystal Structures of Two Barnase Mutants (pdb code 1bao). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the The Contribution of Buried Hydrogen Bonds to Protein Stability: the Crystal Structures of Two Barnase Mutants, PDB code: 1bao:

Zinc binding site 1 out of 1 in 1bao

Go back to Zinc Binding Sites List in 1bao
Zinc binding site 1 out of 1 in the The Contribution of Buried Hydrogen Bonds to Protein Stability: the Crystal Structures of Two Barnase Mutants


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Contribution of Buried Hydrogen Bonds to Protein Stability: the Crystal Structures of Two Barnase Mutants within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn111

b:18.4
occ:0.99
ND1 C:HIS18 2.1 10.5 1.0
CE1 C:HIS18 2.9 10.5 1.0
CG C:HIS18 3.2 11.1 1.0
CB C:HIS18 3.7 12.4 1.0
O C:TYR17 4.0 16.4 1.0
NE2 C:HIS18 4.1 6.3 1.0
O C:HOH167 4.2 17.4 1.0
CD2 C:HIS18 4.3 8.8 1.0
C C:TYR17 4.4 16.0 1.0
O C:HOH112 4.5 3.7 0.5
O C:THR16 4.8 15.1 1.0
N C:HIS18 4.8 15.0 1.0
CA C:HIS18 4.9 15.3 1.0

Reference:

Y.W.Chen, A.R.Fersht, K.Henrick. Contribution of Buried Hydrogen Bonds to Protein Stability. the Crystal Structures of Two Barnase Mutants. J.Mol.Biol. V. 234 1158 1993.
ISSN: ISSN 0022-2836
PubMed: 8263918
DOI: 10.1006/JMBI.1993.1667
Page generated: Sat Oct 12 22:28:36 2024

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