Atomistry » Zinc » PDB 5evk-5f8g » 5f5e
Atomistry »
  Zinc »
    PDB 5evk-5f8g »
      5f5e »

Zinc in PDB 5f5e: The Crystal Structure of MLL1 Set Domain with N3816I/Q3867L Mutation

Enzymatic activity of The Crystal Structure of MLL1 Set Domain with N3816I/Q3867L Mutation

All present enzymatic activity of The Crystal Structure of MLL1 Set Domain with N3816I/Q3867L Mutation:
2.1.1.43;

Protein crystallography data

The structure of The Crystal Structure of MLL1 Set Domain with N3816I/Q3867L Mutation, PDB code: 5f5e was solved by Y.Li, M.Lei, Y.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.07 / 1.80
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 54.574, 54.574, 104.656, 90.00, 90.00, 120.00
R / Rfree (%) 20.2 / 23.6

Zinc Binding Sites:

The binding sites of Zinc atom in the The Crystal Structure of MLL1 Set Domain with N3816I/Q3867L Mutation (pdb code 5f5e). 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 The Crystal Structure of MLL1 Set Domain with N3816I/Q3867L Mutation, PDB code: 5f5e:

Zinc binding site 1 out of 1 in 5f5e

Go back to Zinc Binding Sites List in 5f5e
Zinc binding site 1 out of 1 in the The Crystal Structure of MLL1 Set Domain with N3816I/Q3867L Mutation


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Crystal Structure of MLL1 Set Domain with N3816I/Q3867L Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn4001

b:53.7
occ:1.00
SG A:CYS3957 2.1 53.9 1.0
SG A:CYS3964 2.3 57.8 1.0
SG A:CYS3909 2.4 63.9 1.0
SG A:CYS3959 2.5 56.7 1.0
CB A:CYS3957 2.5 54.2 1.0
O A:HOH4109 2.7 37.3 1.0
C A:CYS3957 3.5 52.1 1.0
CA A:CYS3957 3.6 51.6 1.0
N A:CYS3959 3.7 55.8 1.0
O A:CYS3957 3.7 55.0 1.0
CB A:CYS3959 3.7 65.2 1.0
O A:HOH4114 3.8 43.7 1.0
CB A:CYS3909 3.8 50.7 1.0
CB A:CYS3964 3.9 58.6 1.0
N A:ASN3958 4.0 51.7 1.0
N A:LYS3966 4.2 64.6 1.0
CA A:CYS3959 4.3 59.6 1.0
N A:CYS3909 4.4 49.8 1.0
N A:ARG3965 4.4 69.9 1.0
N A:CYS3957 4.6 54.5 1.0
CA A:CYS3964 4.6 68.9 1.0
C A:ASN3958 4.7 50.7 1.0
CA A:LYS3966 4.7 61.8 1.0
CA A:ASN3958 4.7 52.4 1.0
CA A:CYS3909 4.7 54.8 1.0
O A:HOH4179 4.8 40.4 1.0
C A:CYS3964 4.8 68.9 1.0
N A:GLY3960 4.9 60.9 1.0
C A:LYS3966 4.9 63.7 1.0
CD2 A:HIS3907 5.0 45.8 1.0

Reference:

Y.Li, J.Han, Y.Zhang, F.Cao, Z.Liu, S.Li, J.Wu, C.Hu, Y.Wang, J.Shuai, J.Chen, L.Cao, D.Li, P.Shi, C.Tian, J.Zhang, Y.Dou, G.Li, Y.Chen, M.Lei. Structural Basis For Activity Regulation of Mll Family Methyltransferases. Nature V. 530 447 2016.
ISSN: ESSN 1476-4687
PubMed: 26886794
DOI: 10.1038/NATURE16952
Page generated: Sun Oct 27 15:49:16 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy