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Zinc in PDB 4aa2: Crystal Structure of Ance in Complex with Bradykinin Potentiating Peptide B

Enzymatic activity of Crystal Structure of Ance in Complex with Bradykinin Potentiating Peptide B

All present enzymatic activity of Crystal Structure of Ance in Complex with Bradykinin Potentiating Peptide B:
3.4.15.1;

Protein crystallography data

The structure of Crystal Structure of Ance in Complex with Bradykinin Potentiating Peptide B, PDB code: 4aa2 was solved by R.E.Isaac, M.Akif, S.L.U.Schwager, G.Masuyer, E.D.Sturrock, K.R.Acharya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.10 / 1.99
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 173.214, 173.214, 102.898, 90.00, 90.00, 120.00
R / Rfree (%) 20.325 / 22.578

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Ance in Complex with Bradykinin Potentiating Peptide B (pdb code 4aa2). 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 Ance in Complex with Bradykinin Potentiating Peptide B, PDB code: 4aa2:

Zinc binding site 1 out of 1 in 4aa2

Go back to Zinc Binding Sites List in 4aa2
Zinc binding site 1 out of 1 in the Crystal Structure of Ance in Complex with Bradykinin Potentiating Peptide B


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 Ance in Complex with Bradykinin Potentiating Peptide B within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1616

b:55.7
occ:1.00
OE1 A:GLU395 2.2 31.5 1.0
NE2 A:HIS371 2.2 31.9 1.0
O P:ILE9 2.4 36.4 1.0
NE2 A:HIS367 2.5 35.3 1.0
C P:ILE9 2.9 36.2 1.0
CE1 A:HIS371 3.1 31.2 1.0
CD A:GLU395 3.2 31.8 1.0
CD2 A:HIS371 3.2 30.9 1.0
OE2 A:GLU368 3.3 37.2 1.0
CD2 A:HIS367 3.3 34.6 1.0
CE1 A:HIS367 3.4 35.8 1.0
N P:ILE9 3.5 37.6 1.0
OE2 A:GLU395 3.6 31.9 1.0
N P:PRO10 3.6 35.5 1.0
CA P:ILE9 3.7 36.8 1.0
CA P:PRO10 3.8 35.0 1.0
C P:LYS8 4.0 38.7 1.0
O A:HOH2301 4.1 31.6 1.0
ND1 A:HIS371 4.2 31.2 1.0
CG A:HIS371 4.3 31.4 1.0
CE1 A:TYR507 4.4 29.2 1.0
CD A:GLU368 4.4 35.6 1.0
O P:LYS8 4.4 38.4 1.0
CG A:HIS367 4.4 34.6 1.0
ND1 A:HIS367 4.5 35.5 1.0
CG A:GLU395 4.5 31.2 1.0
OH A:TYR507 4.5 30.4 1.0
CB P:LYS8 4.5 39.7 1.0
CA A:GLU395 4.7 31.1 1.0
C P:PRO10 4.7 34.3 1.0
CB A:GLU395 4.7 31.3 1.0
CA P:LYS8 4.8 39.6 1.0
CD P:PRO10 4.8 35.5 1.0
OE1 A:GLU368 4.8 35.9 1.0
CZ A:TYR507 5.0 29.4 1.0

Reference:

M.Akif, G.Masuyer, R.J.Bingham, E.D.Sturrock, R.E.Isaac, K.R.Acharya. Structural Basis of Peptide Recognition By the Angiotensin-I Converting Enzyme Homologue Ance From Drosophila Melanogaster Febs J. V. 279 4525 2012.
ISSN: ISSN 1742-464X
PubMed: 23082758
DOI: 10.1111/FEBS.12038
Page generated: Wed Dec 16 05:02:55 2020

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