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Zinc in PDB 4afs: Human Chymase - Fynomer Complex

Enzymatic activity of Human Chymase - Fynomer Complex

All present enzymatic activity of Human Chymase - Fynomer Complex:
3.4.21.39;

Protein crystallography data

The structure of Human Chymase - Fynomer Complex, PDB code: 4afs was solved by D.Schlatter, S.Brack, D.W.Banner, S.Batey, J.Benz, J.Bertschinger, W.Huber, C.Joseph, A.Rufer, A.Van Der Kloosters, M.Weber, D.Grabulovski, M.Hennig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.49 / 1.90
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 78.584, 89.072, 48.494, 90.00, 90.00, 90.00
R / Rfree (%) 18.662 / 23.796

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Chymase - Fynomer Complex (pdb code 4afs). 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 Human Chymase - Fynomer Complex, PDB code: 4afs:

Zinc binding site 1 out of 1 in 4afs

Go back to Zinc Binding Sites List in 4afs
Zinc binding site 1 out of 1 in the Human Chymase - Fynomer Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Chymase - Fynomer Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1227

b:39.6
occ:1.00
OE2 A:GLU64 1.8 37.3 1.0
NE2 A:HIS10 1.9 37.5 1.0
O A:HOH2019 2.0 36.2 1.0
CD A:GLU64 2.7 39.3 1.0
CE1 A:HIS10 2.8 32.1 1.0
OE1 A:GLU64 3.0 43.1 1.0
CD2 A:HIS10 3.0 31.9 1.0
ND1 A:HIS10 4.0 34.5 1.0
CG A:GLU64 4.1 36.3 1.0
CG A:HIS10 4.1 34.6 1.0
O A:HOH2058 4.3 43.0 1.0
O A:HOH2052 4.4 33.4 1.0
OG1 A:THR66 4.5 29.9 1.0
CG2 A:THR66 4.6 35.1 1.0
CB A:PRO9 4.7 31.3 1.0
CB A:HIS58 5.0 33.6 1.0

Reference:

D.Schlatter, S.Brack, D.W.Banner, S.Batey, J.Benz, J.Bertschinger, W.Huber, C.Joseph, A.Rufer, A.Van Der Klooster, M.Weber, D.Grabulovski, M.Hennig. Generation, Characterization and Structural Data of Chymase Binding Proteins Based on the Human Fyn Kinase SH3 Domain. Mabs V. 4 497 2012.
ISSN: ISSN 1942-0862
PubMed: 22653218
DOI: 10.4161/MABS.20452
Page generated: Wed Dec 16 05:03:06 2020

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