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Zinc in PDB 8hln: Crystal Structure of P53/BCL2 Fusion Complex(COMPLEX3)

Protein crystallography data

The structure of Crystal Structure of P53/BCL2 Fusion Complex(COMPLEX3), PDB code: 8hln was solved by M.Guo, H.Wei, H.Wang, Y.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.83 / 2.35
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 44.701, 70.528, 127.725, 90, 90, 90
R / Rfree (%) 20.2 / 25.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of P53/BCL2 Fusion Complex(COMPLEX3) (pdb code 8hln). 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 P53/BCL2 Fusion Complex(COMPLEX3), PDB code: 8hln:

Zinc binding site 1 out of 1 in 8hln

Go back to Zinc Binding Sites List in 8hln
Zinc binding site 1 out of 1 in the Crystal Structure of P53/BCL2 Fusion Complex(COMPLEX3)


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 P53/BCL2 Fusion Complex(COMPLEX3) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:30.0
occ:1.00
SG A:CYS238 2.2 46.3 1.0
SG A:CYS242 2.4 44.8 1.0
SG A:CYS176 2.5 49.5 1.0
ND1 A:HIS179 2.6 52.7 1.0
CB A:CYS242 2.7 41.5 1.0
CB A:CYS176 2.9 54.1 1.0
CB A:CYS238 3.2 40.0 1.0
CE1 A:HIS179 3.4 51.5 1.0
N A:CYS176 3.7 42.3 1.0
CG A:HIS179 3.7 49.5 1.0
CA A:CYS176 3.9 44.1 1.0
CA A:CYS238 3.9 43.3 1.0
CB A:HIS179 4.1 42.3 1.0
CA A:CYS242 4.2 45.5 1.0
N A:ASN239 4.5 44.4 1.0
NE2 A:HIS179 4.6 52.9 1.0
O A:ASN239 4.6 39.9 1.0
C A:CYS238 4.7 45.5 1.0
C A:CYS176 4.8 43.6 1.0
CD2 A:HIS179 4.8 52.1 1.0
C A:ARG175 4.9 43.8 1.0
C A:CYS242 4.9 49.6 1.0
O A:CYS176 4.9 42.3 1.0
O A:MET237 5.0 34.8 1.0
N A:HIS179 5.0 39.3 1.0

Reference:

H.Wei, Y.Chen. Structures of P53/Bcl-2 Complex Suggest A Mechanism For P53 to Antagonize Bcl-2 Activity Nat Commun 2023.
ISSN: ESSN 2041-1723
DOI: HTTPS://DOI.ORG/10.1038/S41467-023-40087-2
Page generated: Thu Dec 28 13:11:56 2023

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