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Zinc in PDB 3rsn: Crystal Structure of the N-Terminal Region of Human ASH2L

Protein crystallography data

The structure of Crystal Structure of the N-Terminal Region of Human ASH2L, PDB code: 3rsn was solved by Y.Chen, B.Wan, K.C.Wang, F.Cao, Y.Yang, A.Protacio, Y.Dou, H.Y.Chang, M.Lei, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.06 / 2.10
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 49.984, 49.984, 165.519, 90.00, 90.00, 120.00
R / Rfree (%) 21.3 / 25.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the N-Terminal Region of Human ASH2L (pdb code 3rsn). 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 the N-Terminal Region of Human ASH2L, PDB code: 3rsn:

Zinc binding site 1 out of 1 in 3rsn

Go back to Zinc Binding Sites List in 3rsn
Zinc binding site 1 out of 1 in the Crystal Structure of the N-Terminal Region of Human ASH2L


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 the N-Terminal Region of Human ASH2L within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn200

b:35.2
occ:1.00
SG A:CYS56 2.3 34.8 1.0
SG A:CYS26 2.4 33.5 1.0
SG A:CYS53 2.5 31.6 1.0
SG A:CYS23 2.5 33.9 1.0
CB A:CYS56 3.1 34.8 1.0
CB A:CYS26 3.2 35.2 1.0
CB A:CYS23 3.3 34.3 1.0
N A:CYS26 3.6 37.8 1.0
CB A:CYS53 3.7 32.8 1.0
CA A:CYS26 4.0 38.3 1.0
N A:CYS53 4.0 33.6 1.0
N A:CYS56 4.3 35.9 1.0
CA A:CYS56 4.3 39.4 1.0
CZ A:PHE30 4.3 33.5 1.0
CA A:CYS53 4.4 34.3 1.0
CE1 A:PHE30 4.4 32.2 1.0
CB A:ILE25 4.6 38.2 1.0
C A:ILE25 4.7 39.8 1.0
CA A:CYS23 4.7 36.8 1.0
O A:CYS53 4.9 34.8 1.0
C A:CYS26 4.9 37.6 1.0
C A:CYS53 5.0 35.4 1.0

Reference:

Y.Chen, B.Wan, K.C.Wang, F.Cao, Y.Yang, A.Protacio, Y.Dou, H.Y.Chang, M.Lei. Crystal Structure of the N-Terminal Region of Human ASH2L Shows A Winged-Helix Motif Involved in Dna Binding. Embo Rep. V. 12 797 2011.
ISSN: ISSN 1469-221X
PubMed: 21660059
DOI: 10.1038/EMBOR.2011.101
Page generated: Wed Dec 16 04:47:55 2020

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