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Zinc in PDB 4lof: Human P53 Core Domain Mutant V157F/N235K/N239Y

Protein crystallography data

The structure of Human P53 Core Domain Mutant V157F/N235K/N239Y, PDB code: 4lof was solved by B.D.Wallentine, Y.Wang, H.Luecke, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.15 / 2.00
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 107.268, 51.128, 33.814, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 25.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Human P53 Core Domain Mutant V157F/N235K/N239Y (pdb code 4lof). 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 Human P53 Core Domain Mutant V157F/N235K/N239Y, PDB code: 4lof:

Zinc binding site 1 out of 1 in 4lof

Go back to Zinc Binding Sites List in 4lof
Zinc binding site 1 out of 1 in the Human P53 Core Domain Mutant V157F/N235K/N239Y


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human P53 Core Domain Mutant V157F/N235K/N239Y within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:27.6
occ:1.00
ND1 A:HIS179 2.1 21.2 1.0
SG A:CYS242 2.3 19.8 1.0
SG A:CYS176 2.4 22.6 1.0
SG A:CYS238 2.4 22.7 1.0
CE1 A:HIS179 3.0 26.2 1.0
CB A:CYS242 3.0 21.3 1.0
CG A:HIS179 3.1 25.8 1.0
CB A:CYS238 3.4 16.9 1.0
CB A:CYS176 3.4 22.4 1.0
CB A:HIS179 3.5 20.6 1.0
N A:CYS176 3.9 23.1 1.0
CA A:CYS238 3.9 18.4 1.0
NE2 A:HIS179 4.1 29.0 1.0
CD2 A:HIS179 4.2 27.0 1.0
CA A:CYS176 4.3 21.2 1.0
CA A:CYS242 4.4 19.9 1.0
N A:TYR239 4.5 19.9 1.0
O A:HOH542 4.6 28.6 1.0
O A:MET237 4.6 18.8 1.0
N A:HIS179 4.6 23.9 1.0
CA A:HIS179 4.6 27.5 1.0
O A:HOH545 4.7 30.1 1.0
O A:CYS176 4.8 24.4 1.0
C A:CYS238 4.8 20.0 1.0
C A:CYS176 4.9 22.2 1.0

Reference:

B.D.Wallentine, Y.Wang, V.Tretyachenko-Ladokhina, M.Tan, D.F.Senear, H.Luecke. Structures of Oncogenic, Suppressor and Rescued P53 Core-Domain Variants: Mechanisms of Mutant P53 Rescue. Acta Crystallogr.,Sect.D V. 69 2146 2013.
ISSN: ISSN 0907-4449
PubMed: 24100332
DOI: 10.1107/S0907444913020830
Page generated: Wed Dec 16 05:33:38 2020

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