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Zinc in PDB 4mzi: Crystal Structure of A Human Mutant P53

Protein crystallography data

The structure of Crystal Structure of A Human Mutant P53, PDB code: 4mzi was solved by S.Emamzadah, L.Tropia, I.Vincenti, B.Falquet, T.D.Halazonetis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.25
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 44.707, 62.428, 73.701, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 20.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of A Human Mutant P53 (pdb code 4mzi). 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 Crystal Structure of A Human Mutant P53, PDB code: 4mzi:

Zinc binding site 1 out of 1 in 4mzi

Go back to Zinc Binding Sites List in 4mzi
Zinc binding site 1 out of 1 in the Crystal Structure of A Human Mutant P53


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of A Human Mutant P53 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:10.6
occ:1.00
SG A:CYS176 2.3 11.1 1.0
SG A:CYS238 2.4 10.2 1.0
SG A:CYS242 2.4 11.0 1.0
CD2 A:HIS179 2.7 22.7 1.0
CB A:CYS242 3.2 12.0 1.0
CB A:CYS238 3.4 9.8 1.0
CB A:CYS176 3.4 11.8 1.0
CG A:HIS179 3.4 19.0 1.0
CB A:HIS179 3.5 13.5 1.0
CA A:CYS238 3.8 8.0 1.0
NE2 A:HIS179 3.9 23.6 1.0
N A:CYS176 4.0 10.5 1.0
CA A:CYS176 4.3 11.1 1.0
N A:ASN239 4.4 9.0 1.0
N A:HIS179 4.4 13.4 1.0
CA A:CYS242 4.6 11.5 1.0
O A:MET237 4.6 8.7 1.0
CA A:HIS179 4.6 13.8 1.0
ND1 A:HIS179 4.7 24.6 1.0
O A:HOH435 4.7 11.9 1.0
C A:CYS238 4.7 8.7 1.0
O A:HOH581 4.8 24.9 1.0
CE1 A:HIS179 4.9 26.3 1.0
C A:CYS176 4.9 12.3 1.0
O A:CYS176 4.9 12.8 1.0
N A:CYS238 5.0 7.8 1.0

Reference:

S.Emamzadah, L.Tropia, I.Vincenti, B.Falquet, T.D.Halazonetis. Reversal of the Dna-Binding-Induced Loop L1 Conformational Switch in An Engineered Human P53 Protein. J.Mol.Biol. V. 426 936 2014.
ISSN: ISSN 0022-2836
PubMed: 24374182
DOI: 10.1016/J.JMB.2013.12.020
Page generated: Wed Dec 16 05:36:13 2020

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