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Zinc in PDB 2bin: Human P53 Core Domain Mutant M133L-H168R-V203A-N239Y-N268D

Protein crystallography data

The structure of Human P53 Core Domain Mutant M133L-H168R-V203A-N239Y-N268D, PDB code: 2bin was solved by A.C.Joerger, A.R.Fersht, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 55.0 / 1.9
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 45.045, 45.045, 331.780, 90.00, 90.00, 120.00
R / Rfree (%) 19.9 / 23.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Human P53 Core Domain Mutant M133L-H168R-V203A-N239Y-N268D (pdb code 2bin). 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 M133L-H168R-V203A-N239Y-N268D, PDB code: 2bin:

Zinc binding site 1 out of 1 in 2bin

Go back to Zinc Binding Sites List in 2bin
Zinc binding site 1 out of 1 in the Human P53 Core Domain Mutant M133L-H168R-V203A-N239Y-N268D


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 M133L-H168R-V203A-N239Y-N268D within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1292

b:24.2
occ:1.00
ND1 A:HIS179 2.0 19.1 1.0
SG A:CYS242 2.4 25.4 1.0
SG A:CYS238 2.4 24.6 1.0
SG A:CYS176 2.4 23.8 1.0
CE1 A:HIS179 2.9 20.3 1.0
CB A:CYS242 3.1 24.7 1.0
CG A:HIS179 3.1 22.0 1.0
CB A:CYS176 3.4 26.6 1.0
CB A:HIS179 3.5 25.7 1.0
CB A:CYS238 3.6 24.3 1.0
CA A:CYS238 3.9 21.5 1.0
N A:TYR239 4.0 20.1 1.0
N A:CYS176 4.0 26.5 1.0
NE2 A:HIS179 4.1 23.7 1.0
CD2 A:HIS179 4.2 24.5 1.0
CA A:CYS176 4.3 25.1 1.0
N A:HIS179 4.3 25.4 1.0
C A:CYS238 4.5 24.3 1.0
CA A:CYS242 4.5 34.0 1.0
O A:HOH2106 4.5 31.5 1.0
CA A:HIS179 4.6 28.2 1.0
O A:TYR239 4.9 22.3 1.0
O A:CYS176 4.9 21.1 1.0
C A:CYS176 4.9 25.9 1.0

Reference:

A.C.Joerger, H.C.Ang, D.B.Veprintsev, C.M.Blair, A.R.Fersht. Structures of P53 Cancer Mutants and Mechanism of Rescue By Second-Site Suppressor Mutations J.Biol.Chem. V. 280 16030 2005.
ISSN: ISSN 0021-9258
PubMed: 15703170
DOI: 10.1074/JBC.M500179200
Page generated: Wed Dec 16 03:18:27 2020

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