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Zinc in PDB 1r4v: 1.9A Crystal Structure of Protein AQ328 From Aquifex Aeolicus

Protein crystallography data

The structure of 1.9A Crystal Structure of Protein AQ328 From Aquifex Aeolicus, PDB code: 1r4v was solved by Y.Qiu, V.Tereshko, Y.Kim, R.Zhang, F.Collart, A.Joachimiak, A.Kossiakoff, Midwest Center For Structural Genomics (Mcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.90
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 56.036, 56.036, 244.768, 90.00, 90.00, 120.00
R / Rfree (%) 18.1 / 21.3

Other elements in 1r4v:

The structure of 1.9A Crystal Structure of Protein AQ328 From Aquifex Aeolicus also contains other interesting chemical elements:

Arsenic (As) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the 1.9A Crystal Structure of Protein AQ328 From Aquifex Aeolicus (pdb code 1r4v). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the 1.9A Crystal Structure of Protein AQ328 From Aquifex Aeolicus, PDB code: 1r4v:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in 1r4v

Go back to Zinc Binding Sites List in 1r4v
Zinc binding site 1 out of 3 in the 1.9A Crystal Structure of Protein AQ328 From Aquifex Aeolicus


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of 1.9A Crystal Structure of Protein AQ328 From Aquifex Aeolicus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn201

b:27.1
occ:1.00
OE2 A:GLU158 2.0 29.9 1.0
OE1 A:GLU161 2.1 26.0 1.0
CD A:GLU158 2.8 29.1 1.0
OE2 A:GLU161 2.8 29.4 1.0
CD A:GLU161 2.8 20.5 1.0
OE1 A:GLU158 2.8 38.3 1.0
O A:HOH392 4.2 36.8 1.0
CG A:GLU161 4.2 21.5 1.0
CG A:GLU158 4.2 27.4 1.0
CD A:ARG157 4.3 30.0 1.0
NH1 A:ARG157 4.4 33.3 1.0
CB A:GLU161 4.7 18.6 1.0

Zinc binding site 2 out of 3 in 1r4v

Go back to Zinc Binding Sites List in 1r4v
Zinc binding site 2 out of 3 in the 1.9A Crystal Structure of Protein AQ328 From Aquifex Aeolicus


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of 1.9A Crystal Structure of Protein AQ328 From Aquifex Aeolicus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn202

b:43.7
occ:1.00
O1 A:CAC203 2.0 34.5 1.0
OD2 A:ASP33 2.0 36.8 1.0
O A:HOH514 2.0 22.3 0.5
O A:HOH520 2.1 19.3 0.5
CG A:ASP33 3.0 25.2 1.0
O A:HOH518 3.1 27.7 0.5
OD1 A:ASP33 3.3 34.2 1.0
AS A:CAC203 3.4 32.5 1.0
C2 A:CAC203 3.7 35.6 1.0
OE2 A:GLU21 3.8 60.8 1.0
O A:HOH521 3.8 22.7 0.5
NH2 A:ARG37 3.8 36.9 1.0
NH1 A:ARG25 3.9 28.8 1.0
O A:HOH353 4.2 31.1 1.0
CB A:ASP33 4.3 23.6 1.0
NH2 A:ARG25 4.3 35.1 1.0
CZ A:ARG25 4.5 29.8 1.0
O2 A:CAC203 4.5 40.3 1.0
CD A:GLU21 4.6 57.6 1.0
CG A:GLU21 4.7 55.8 1.0
C1 A:CAC203 4.9 35.9 1.0
O A:HOH471 4.9 58.2 1.0
CZ A:ARG37 5.0 36.9 1.0

Zinc binding site 3 out of 3 in 1r4v

Go back to Zinc Binding Sites List in 1r4v
Zinc binding site 3 out of 3 in the 1.9A Crystal Structure of Protein AQ328 From Aquifex Aeolicus


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of 1.9A Crystal Structure of Protein AQ328 From Aquifex Aeolicus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn204

b:33.5
occ:0.50
OD2 A:ASP46 2.0 40.8 1.0
OE1 A:GLU21 2.0 51.8 1.0
O A:HOH452 2.7 53.2 1.0
CG A:ASP46 3.0 33.7 1.0
CD A:GLU21 3.3 57.6 1.0
OD1 A:ASP46 3.3 36.2 1.0
CG A:ARG25 3.7 38.9 1.0
O A:HOH372 3.7 43.6 1.0
NE A:ARG25 3.7 37.7 1.0
CD A:ARG25 3.9 37.6 1.0
OE2 A:GLU21 4.0 60.8 1.0
CB A:ARG25 4.3 39.8 1.0
O A:HOH483 4.3 52.4 1.0
CB A:GLU21 4.3 54.8 1.0
CG A:GLU21 4.3 55.8 1.0
O A:HOH457 4.4 41.8 1.0
CB A:ASP46 4.4 28.9 1.0
CZ A:ARG25 4.5 29.8 1.0
CA A:GLU21 4.7 54.5 1.0
NH2 A:ARG25 4.9 35.1 1.0
CA A:ARG25 4.9 39.9 1.0

Reference:

Y.Qiu, V.Tereshko, Y.Kim, R.Zhang, F.Collart, M.Yousef, A.Kossiakoff, A.Joachimiak. The Crystal Structure of AQ_328 From the Hyperthermophilic Bacteria Aquifex Aeolicus Shows An Ancestral Histone Fold. Proteins V. 62 8 2006.
ISSN: ISSN 0887-3585
PubMed: 16287087
DOI: 10.1002/PROT.20590
Page generated: Wed Dec 16 03:02:30 2020

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