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Zinc in PDB 3s32: Crystal Structure of ASH2L N-Terminal Domain

Protein crystallography data

The structure of Crystal Structure of ASH2L N-Terminal Domain, PDB code: 3s32 was solved by S.Sarvan, V.Avdic, V.Tremblay, C.-P.Chaturvedi, P.Zhang, S.Lanouette, A.Blais, J.S.Brunzelle, M.Brand, J.-F.Couture, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.95 / 2.45
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 49.893, 49.893, 167.542, 90.00, 90.00, 120.00
R / Rfree (%) 22.5 / 26.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of ASH2L N-Terminal Domain (pdb code 3s32). 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 ASH2L N-Terminal Domain, PDB code: 3s32:

Zinc binding site 1 out of 1 in 3s32

Go back to Zinc Binding Sites List in 3s32
Zinc binding site 1 out of 1 in the Crystal Structure of ASH2L N-Terminal Domain


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 ASH2L N-Terminal Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1

b:68.1
occ:1.00
SG A:CYS150 2.1 40.2 1.0
SG A:CYS120 2.3 41.1 1.0
SG A:CYS147 2.4 38.4 1.0
SG A:CYS117 2.4 46.3 1.0
CB A:CYS150 3.1 43.7 1.0
CB A:CYS117 3.1 44.0 1.0
CB A:CYS120 3.1 44.4 1.0
CB A:CYS147 3.6 37.3 1.0
N A:CYS120 3.7 46.2 1.0
N A:CYS147 3.9 38.6 1.0
CA A:CYS120 4.0 45.5 1.0
CZ A:PHE124 4.2 41.6 1.0
CA A:CYS147 4.3 37.4 1.0
CA A:CYS150 4.4 46.0 1.0
N A:CYS150 4.5 45.8 1.0
CE2 A:PHE124 4.5 38.8 1.0
CA A:CYS117 4.6 42.8 1.0
C A:ILE119 4.8 47.1 1.0
CB A:ILE119 4.8 46.8 1.0
C A:CYS120 4.9 45.1 1.0
N A:ILE119 4.9 44.9 1.0
C A:CYS147 4.9 37.9 1.0

Reference:

S.Sarvan, V.Avdic, V.Tremblay, C.P.Chaturvedi, P.Zhang, S.Lanouette, A.Blais, J.S.Brunzelle, M.Brand, J.F.Couture. Crystal Structure of the Trithorax Group Protein ASH2L Reveals A Forkhead-Like Dna Binding Domain. Nat.Struct.Mol.Biol. V. 18 857 2011.
ISSN: ISSN 1545-9993
PubMed: 21642971
DOI: 10.1038/NSMB.2093
Page generated: Wed Dec 16 04:49:20 2020

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