Zinc in PDB 6znc: Structural Basis of Reactivation of Oncogenic P53 Mutants By A Small Molecule: Methylene Quinuclidinone (Mq). Human Wild-Type P53DBD Bound to Dna and Mq: Wt-Dna-Mq (I)

Protein crystallography data

The structure of Structural Basis of Reactivation of Oncogenic P53 Mutants By A Small Molecule: Methylene Quinuclidinone (Mq). Human Wild-Type P53DBD Bound to Dna and Mq: Wt-Dna-Mq (I), PDB code: 6znc was solved by H.Rozenberg, O.Degtjarik, Y.Diskin-Posner, Z.Shakked, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.61 / 1.64
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 137.744, 49.537, 34.066, 90, 92.79, 90
R / Rfree (%) 16.1 / 19

Zinc Binding Sites:

The binding sites of Zinc atom in the Structural Basis of Reactivation of Oncogenic P53 Mutants By A Small Molecule: Methylene Quinuclidinone (Mq). Human Wild-Type P53DBD Bound to Dna and Mq: Wt-Dna-Mq (I) (pdb code 6znc). 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 Structural Basis of Reactivation of Oncogenic P53 Mutants By A Small Molecule: Methylene Quinuclidinone (Mq). Human Wild-Type P53DBD Bound to Dna and Mq: Wt-Dna-Mq (I), PDB code: 6znc:

Zinc binding site 1 out of 1 in 6znc

Go back to Zinc Binding Sites List in 6znc
Zinc binding site 1 out of 1 in the Structural Basis of Reactivation of Oncogenic P53 Mutants By A Small Molecule: Methylene Quinuclidinone (Mq). Human Wild-Type P53DBD Bound to Dna and Mq: Wt-Dna-Mq (I)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural Basis of Reactivation of Oncogenic P53 Mutants By A Small Molecule: Methylene Quinuclidinone (Mq). Human Wild-Type P53DBD Bound to Dna and Mq: Wt-Dna-Mq (I) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:16.7
occ:1.00
ND1 A:HIS179 2.0 17.3 1.0
SG A:CYS238 2.3 17.3 1.0
SG A:CYS176 2.3 18.2 1.0
SG A:CYS242 2.3 17.1 1.0
CE1 A:HIS179 2.9 17.3 1.0
CG A:HIS179 3.1 17.9 1.0
CB A:CYS242 3.1 17.4 1.0
CB A:CYS238 3.2 13.4 1.0
CB A:CYS176 3.4 18.3 1.0
CB A:HIS179 3.5 18.2 1.0
CA A:CYS238 3.8 17.2 1.0
NE2 A:HIS179 4.1 22.4 1.0
N A:CYS176 4.1 16.5 1.0
CD2 A:HIS179 4.2 21.1 1.0
CA A:CYS176 4.3 17.4 1.0
N A:HIS179 4.3 19.8 1.0
O A:MET237 4.5 19.3 1.0
N A:ASN239 4.5 17.2 1.0
CA A:CYS242 4.6 15.7 1.0
CA A:HIS179 4.6 19.5 1.0
C A:CYS238 4.7 17.5 1.0
O A:HOH458 4.8 19.0 1.0
N A:CYS238 4.9 13.1 1.0
O A:CYS176 4.9 17.9 1.0
C A:CYS176 4.9 14.4 1.0

Reference:

O.Degtjarik, D.Golovenko, Y.Diskin-Posner, L.Abrahmsen, H.Rozenberg, Z.Shakked. P53 Structure 11 To Be Published.
Page generated: Fri Dec 17 11:45:30 2021

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