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Zinc in PDB 2mej: Solution Structure of the Complex Between Bcl-Xl and the P53 Core Domain Determined with Pre Restraints

Zinc Binding Sites:

The binding sites of Zinc atom in the Solution Structure of the Complex Between Bcl-Xl and the P53 Core Domain Determined with Pre Restraints (pdb code 2mej). 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 Solution Structure of the Complex Between Bcl-Xl and the P53 Core Domain Determined with Pre Restraints, PDB code: 2mej:

Zinc binding site 1 out of 1 in 2mej

Go back to Zinc Binding Sites List in 2mej
Zinc binding site 1 out of 1 in the Solution Structure of the Complex Between Bcl-Xl and the P53 Core Domain Determined with Pre Restraints


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Solution Structure of the Complex Between Bcl-Xl and the P53 Core Domain Determined with Pre Restraints within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn401

b:17.1
occ:1.00
HD1 B:HIS179 1.4 0.2 1.0
SG B:CYS176 1.6 0.3 1.0
HG B:CYS242 2.0 1.2 1.0
H B:CYS176 2.4 0.2 1.0
ND1 B:HIS179 2.4 0.2 1.0
SG B:CYS242 2.6 0.2 1.0
HG B:CYS176 2.6 1.1 1.0
CB B:CYS176 3.0 0.2 1.0
N B:CYS176 3.2 0.1 1.0
CB B:CYS242 3.2 0.2 1.0
CE1 B:HIS179 3.3 0.2 1.0
SG B:CYS238 3.3 0.2 1.0
CG B:HIS179 3.4 0.2 1.0
CA B:CYS176 3.7 0.2 1.0
HG B:CYS238 3.7 0.2 1.0
CB B:HIS179 3.8 0.1 1.0
H B:ASN239 3.8 0.2 1.0
CB B:CYS238 3.9 0.1 1.0
OD2 A:ASP159 4.1 0.2 1.0
C B:ARG175 4.2 0.1 1.0
OE2 A:GLU156 4.3 0.2 1.0
CG A:LYS160 4.4 0.2 1.0
CA B:ARG175 4.4 0.1 1.0
NE2 B:HIS179 4.5 0.2 1.0
CA B:CYS238 4.5 0.1 1.0
CA B:CYS242 4.5 0.1 1.0
CD2 B:HIS179 4.5 0.2 1.0
CB B:ARG175 4.6 0.1 1.0
C B:CYS176 4.6 0.1 1.0
N B:ASN239 4.7 0.1 1.0
O B:CYS176 4.8 0.1 1.0
HE B:ARG175 4.8 0.2 1.0
O A:ASP159 4.8 0.1 1.0
CG A:ASP159 4.9 0.2 1.0

Reference:

A.V.Follis, F.Llambi, L.Ou, K.Baran, D.R.Green, R.W.Kriwacki. The Dna-Binding Domain Mediates Both Nuclear and Cytosolic Functions of P53. Nat.Struct.Mol.Biol. V. 21 535 2014.
ISSN: ISSN 1545-9993
PubMed: 24814347
DOI: 10.1038/NSMB.2829
Page generated: Wed Dec 16 03:40:09 2020

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