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Zinc in PDB 4faj: Structure and Mode of Peptide Binding of Pheromone Receptor Prgz

Protein crystallography data

The structure of Structure and Mode of Peptide Binding of Pheromone Receptor Prgz, PDB code: 4faj was solved by R.P.-A.Berntsson, G.K.Schuurman-Wolters, K.Dunny, D.J.Slotboom, B.Poolman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 68.622, 74.122, 112.622, 90.00, 90.00, 90.00
R / Rfree (%) 15.6 / 19.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure and Mode of Peptide Binding of Pheromone Receptor Prgz (pdb code 4faj). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Structure and Mode of Peptide Binding of Pheromone Receptor Prgz, PDB code: 4faj:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 4faj

Go back to Zinc Binding Sites List in 4faj
Zinc binding site 1 out of 4 in the Structure and Mode of Peptide Binding of Pheromone Receptor Prgz


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure and Mode of Peptide Binding of Pheromone Receptor Prgz within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn603

b:32.5
occ:1.00
OD2 A:ASP266 2.0 31.0 1.0
OD2 A:ASP263 2.1 22.8 1.0
CG A:ASP263 2.9 21.2 1.0
OD1 A:ASP263 2.9 23.6 1.0
CG A:ASP266 2.9 26.1 1.0
OD1 A:ASP266 3.5 28.5 1.0
NZ A:LYS559 3.7 31.7 1.0
CB A:ASP266 3.9 23.8 1.0
NZ A:LYS558 4.1 17.1 1.0
CB A:ASP263 4.3 20.5 1.0
NZ A:LYS265 4.4 31.5 1.0
CE A:LYS558 4.5 17.7 1.0
CE A:LYS559 4.8 28.6 1.0
CH2 A:TRP262 4.8 19.9 1.0
O A:HOH933 4.9 32.5 1.0

Zinc binding site 2 out of 4 in 4faj

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Zinc binding site 2 out of 4 in the Structure and Mode of Peptide Binding of Pheromone Receptor Prgz


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure and Mode of Peptide Binding of Pheromone Receptor Prgz within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn604

b:16.9
occ:1.00
OE2 A:GLU279 2.0 16.9 1.0
OH A:TYR301 2.0 15.1 1.0
OE2 A:GLU421 2.0 14.4 1.0
CD A:GLU421 2.7 14.8 1.0
OE1 A:GLU421 2.8 13.8 1.0
CD A:GLU279 2.8 17.1 1.0
OE1 A:GLU279 3.0 16.3 1.0
CZ A:TYR301 3.0 15.8 1.0
CE2 A:TYR301 3.4 15.1 1.0
CG A:GLU421 4.0 15.3 1.0
CE1 A:TYR301 4.2 16.5 1.0
CB A:ASN281 4.2 16.3 1.0
CG A:GLU279 4.3 17.8 1.0
N A:ASN281 4.3 16.1 1.0
N A:ILE280 4.6 16.9 1.0
C1 A:GOL607 4.8 59.6 1.0
CD2 A:TYR301 4.8 15.4 1.0
CA A:ASN281 4.9 16.3 1.0

Zinc binding site 3 out of 4 in 4faj

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Zinc binding site 3 out of 4 in the Structure and Mode of Peptide Binding of Pheromone Receptor Prgz


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structure and Mode of Peptide Binding of Pheromone Receptor Prgz within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn605

b:93.3
occ:1.00
OD1 A:ASP357 2.2 31.2 1.0
CG A:ASP357 3.0 27.8 1.0
NZ A:LYS306 3.1 31.9 1.0
OD2 A:ASP357 3.2 31.9 1.0
O A:LYS353 4.3 27.4 1.0
CE A:LYS306 4.4 30.9 1.0
CB A:ASP357 4.4 25.1 1.0
O A:HOH1057 4.7 49.0 1.0
CE A:LYS303 4.7 31.1 1.0
CD A:LYS306 4.9 31.2 1.0
CA A:ASP357 4.9 24.1 1.0
O A:ASP357 4.9 23.8 1.0

Zinc binding site 4 out of 4 in 4faj

Go back to Zinc Binding Sites List in 4faj
Zinc binding site 4 out of 4 in the Structure and Mode of Peptide Binding of Pheromone Receptor Prgz


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Structure and Mode of Peptide Binding of Pheromone Receptor Prgz within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn606

b:72.1
occ:1.00
OE2 A:GLU370 2.2 33.5 1.0
OE1 A:GLU370 2.7 33.1 1.0
CD A:GLU370 2.7 28.4 1.0
OD2 A:ASP380 4.2 16.9 1.0
CG A:GLU370 4.2 23.7 1.0
O A:HOH1068 5.0 46.8 1.0

Reference:

R.P.Berntsson, G.K.Schuurman-Wolters, G.Dunny, D.J.Slotboom, B.Poolman. Structure and Mode of Peptide Binding of Pheromone Receptor Prgz. J.Biol.Chem. V. 287 37165 2012.
ISSN: ISSN 0021-9258
PubMed: 22948145
DOI: 10.1074/JBC.M112.386334
Page generated: Sat Oct 26 22:21:28 2024

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