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Zinc in PDB 6s1z: Crystal Structure of Anopheles Gambiae ANOACE2 in Complex with Fosinoprilat

Protein crystallography data

The structure of Crystal Structure of Anopheles Gambiae ANOACE2 in Complex with Fosinoprilat, PDB code: 6s1z was solved by G.E.Cozier, K.R.Acharya, J.S.Cashman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 72.19 / 2.50
Space group P 62 2 2
Cell size a, b, c (Å), α, β, γ (°) 166.718, 166.718, 117.458, 90.00, 90.00, 120.00
R / Rfree (%) 29.4 / 33.7

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Anopheles Gambiae ANOACE2 in Complex with Fosinoprilat (pdb code 6s1z). 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 Anopheles Gambiae ANOACE2 in Complex with Fosinoprilat, PDB code: 6s1z:

Zinc binding site 1 out of 1 in 6s1z

Go back to Zinc Binding Sites List in 6s1z
Zinc binding site 1 out of 1 in the Crystal Structure of Anopheles Gambiae ANOACE2 in Complex with Fosinoprilat


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 Anopheles Gambiae ANOACE2 in Complex with Fosinoprilat within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn705

b:87.4
occ:1.00
NE2 A:HIS387 1.9 0.1 1.0
OE2 A:GLU411 2.0 83.8 1.0
NE2 A:HIS383 2.0 63.1 1.0
O01 A:KS8704 2.2 91.2 1.0
HE1 A:HIS383 2.3 92.2 1.0
CE1 A:HIS383 2.4 76.7 1.0
CE1 A:HIS387 2.8 94.2 1.0
CD A:GLU411 2.9 88.6 1.0
HE1 A:HIS387 3.0 0.1 1.0
CD2 A:HIS387 3.0 100.0 1.0
HA A:GLU411 3.2 99.5 1.0
CD2 A:HIS383 3.2 74.2 1.0
HH A:TYR523 3.3 1.0 1.0
HD2 A:HIS387 3.3 0.1 1.0
P02 A:KS8704 3.3 80.9 1.0
OE1 A:GLU411 3.4 74.4 1.0
O03 A:KS8704 3.4 93.8 1.0
HE2 A:TYR523 3.5 0.1 1.0
HB3 A:GLU411 3.5 99.4 1.0
ND1 A:HIS383 3.6 50.4 1.0
HD2 A:HIS383 3.7 89.2 1.0
OH A:TYR523 3.8 89.8 1.0
CE2 A:TYR523 3.9 84.9 1.0
CG A:GLU411 4.0 87.7 1.0
ND1 A:HIS387 4.0 90.6 1.0
CB A:GLU411 4.0 82.7 1.0
CA A:GLU411 4.0 82.8 1.0
CG A:HIS383 4.0 73.8 1.0
CG A:HIS387 4.1 0.2 1.0
CZ A:TYR523 4.1 79.8 1.0
H052 A:KS8704 4.3 0.6 1.0
H051 A:KS8704 4.3 0.6 1.0
H141 A:KS8704 4.3 94.9 1.0
HG3 A:GLU411 4.4 0.4 1.0
C14 A:KS8704 4.4 78.9 1.0
C05 A:KS8704 4.7 85.4 1.0
HG2 A:GLU411 4.7 0.4 1.0
C04 A:KS8704 4.7 92.6 1.0
HD1 A:HIS387 4.7 0.9 1.0
C15 A:KS8704 4.7 79.3 1.0
N A:GLU411 4.8 86.1 1.0
O16 A:KS8704 4.8 63.5 1.0
CD2 A:TYR523 4.8 68.0 1.0
HB2 A:GLU411 4.9 99.4 1.0
O A:HIS383 5.0 0.9 1.0

Reference:

J.S.Cashman, G.E.Cozier, C.Harrison, R.E.Isaac, K.R.Acharya. Crystal Structures of Angiotensin-Converting Enzyme From Anopheles Gambiae in Its Native Form and with A Bound Inhibitor. Biochem.J. V. 476 3505 2019.
ISSN: ESSN 1470-8728
PubMed: 31682720
DOI: 10.1042/BCJ20190635
Page generated: Tue Oct 29 07:00:24 2024

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