Zinc in PDB 5wak: Crystal Structure of A SUZ12-RBBP4 Binary Complex

Protein crystallography data

The structure of Crystal Structure of A SUZ12-RBBP4 Binary Complex, PDB code: 5wak was solved by S.Chen, L.Jiao, X.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.76 / 3.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 105.976, 107.696, 107.769, 90.00, 90.00, 90.00
R / Rfree (%) 17.8 / 25.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of A SUZ12-RBBP4 Binary Complex (pdb code 5wak). 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 A SUZ12-RBBP4 Binary Complex, PDB code: 5wak:

Zinc binding site 1 out of 1 in 5wak

Go back to Zinc Binding Sites List in 5wak
Zinc binding site 1 out of 1 in the Crystal Structure of A SUZ12-RBBP4 Binary Complex


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 A SUZ12-RBBP4 Binary Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1001

b:52.8
occ:1.00
NE2 B:HIS471 2.0 49.2 1.0
NE2 B:HIS466 2.1 40.8 1.0
SG B:CYS453 2.2 54.4 1.0
SG B:CYS450 2.2 47.0 1.0
CE1 B:HIS466 2.9 38.5 1.0
CD2 B:HIS471 3.0 49.6 1.0
CE1 B:HIS471 3.0 49.4 1.0
CB B:CYS453 3.0 52.9 1.0
CD2 B:HIS466 3.2 40.7 1.0
CB B:CYS450 3.4 44.0 1.0
N B:CYS453 3.5 58.5 1.0
CA B:CYS453 3.8 56.2 1.0
CG B:HIS471 4.1 48.1 1.0
ND1 B:HIS466 4.1 37.4 1.0
ND1 B:HIS471 4.1 50.5 1.0
CG B:HIS466 4.2 36.0 1.0
C B:TRP452 4.5 63.8 1.0
C B:CYS453 4.6 60.1 1.0
CB B:TRP452 4.7 54.3 1.0
CA B:CYS450 4.8 47.4 1.0
CB B:CYS470 4.8 42.3 1.0
N B:TRP452 4.9 56.7 1.0
CA B:TRP452 4.9 57.0 1.0
CD2 B:LEU467 5.0 43.6 1.0

Reference:

S.Chen, L.Jiao, M.Shubbar, X.Yang, X.Liu. Unique Structural Platforms of SUZ12 Dictate Distinct Classes of PRC2 For Chromatin Binding. Mol. Cell V. 69 840 2018.
ISSN: ISSN 1097-4164
PubMed: 29499137
DOI: 10.1016/J.MOLCEL.2018.01.039
Page generated: Wed Dec 16 11:15:41 2020

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