Atomistry » Zinc » PDB 4yyt-4zfr » 4z40
Atomistry »
  Zinc »
    PDB 4yyt-4zfr »
      4z40 »

Zinc in PDB 4z40: Active Site Complex Bambc of Benzoyl Coenzyme A Reductase As Isolated

Protein crystallography data

The structure of Active Site Complex Bambc of Benzoyl Coenzyme A Reductase As Isolated, PDB code: 4z40 was solved by T.Weinert, J.W.Kung, S.Weidenweber, S.G.Huwiler, M.Boll, U.Ermler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.50 / 2.35
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 125.190, 116.820, 143.600, 90.00, 110.39, 90.00
R / Rfree (%) 21.2 / 23.8

Other elements in 4z40:

The structure of Active Site Complex Bambc of Benzoyl Coenzyme A Reductase As Isolated also contains other interesting chemical elements:

Tungsten (W) 4 atoms
Magnesium (Mg) 4 atoms
Iron (Fe) 64 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Active Site Complex Bambc of Benzoyl Coenzyme A Reductase As Isolated (pdb code 4z40). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Active Site Complex Bambc of Benzoyl Coenzyme A Reductase As Isolated, PDB code: 4z40:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 4z40

Go back to Zinc Binding Sites List in 4z40
Zinc binding site 1 out of 4 in the Active Site Complex Bambc of Benzoyl Coenzyme A Reductase As Isolated


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Active Site Complex Bambc of Benzoyl Coenzyme A Reductase As Isolated within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn707

b:65.5
occ:0.17
OE1 A:GLU257 2.0 0.8 1.0
OE1 A:GLU251 2.0 0.2 1.0
NE2 A:HIS255 2.0 0.9 1.0
ND1 A:HIS260 2.0 0.4 1.0
CD A:GLU257 2.5 0.2 1.0
CD A:GLU251 2.7 0.6 1.0
OE2 A:GLU251 2.7 0.1 1.0
OE2 A:GLU257 2.7 0.2 1.0
CE1 A:HIS260 2.7 0.2 1.0
CE1 A:HIS255 2.8 0.4 1.0
CD2 A:HIS255 3.2 0.4 1.0
CG A:HIS260 3.2 0.1 1.0
CG A:GLU257 3.8 1.0 1.0
CB A:HIS260 3.8 0.8 1.0
ND1 A:HIS255 3.9 0.2 1.0
NE2 A:HIS260 4.0 0.5 1.0
CG A:GLU251 4.2 0.3 1.0
CG A:HIS255 4.2 0.4 1.0
CD2 A:HIS260 4.2 0.6 1.0
CD1 A:LEU326 4.2 0.5 1.0
CB A:GLU257 4.3 0.3 1.0
CA A:GLU257 4.3 0.1 1.0
NZ A:LYS325 4.9 0.6 1.0

Zinc binding site 2 out of 4 in 4z40

Go back to Zinc Binding Sites List in 4z40
Zinc binding site 2 out of 4 in the Active Site Complex Bambc of Benzoyl Coenzyme A Reductase As Isolated


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Active Site Complex Bambc of Benzoyl Coenzyme A Reductase As Isolated within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn707

b:57.5
occ:0.26
OE1 B:GLU257 1.9 0.1 1.0
OE1 B:GLU251 2.0 84.8 1.0
NE2 B:HIS255 2.1 0.0 1.0
ND1 B:HIS260 2.1 0.2 1.0
CD B:GLU257 2.4 0.8 1.0
OE2 B:GLU251 2.6 81.1 1.0
OE2 B:GLU257 2.6 0.2 1.0
CD B:GLU251 2.6 82.1 1.0
CE1 B:HIS255 2.8 0.2 1.0
CE1 B:HIS260 2.8 0.7 1.0
CD2 B:HIS255 3.2 0.3 1.0
CG B:HIS260 3.3 0.0 1.0
CG B:GLU257 3.7 0.6 1.0
CB B:HIS260 3.9 0.2 1.0
ND1 B:HIS255 3.9 0.2 1.0
NE2 B:HIS260 4.1 0.8 1.0
CG B:GLU251 4.1 80.2 1.0
CD1 B:LEU326 4.2 80.6 1.0
CG B:HIS255 4.2 0.7 1.0
CB B:GLU257 4.2 0.6 1.0
CA B:GLU257 4.3 1.0 1.0
CD2 B:HIS260 4.3 0.1 1.0
NZ B:LYS325 4.8 86.2 1.0
CG B:LEU326 4.9 79.8 1.0
CD2 B:LEU326 5.0 79.2 1.0
CB B:GLU251 5.0 78.9 1.0

Zinc binding site 3 out of 4 in 4z40

Go back to Zinc Binding Sites List in 4z40
Zinc binding site 3 out of 4 in the Active Site Complex Bambc of Benzoyl Coenzyme A Reductase As Isolated


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Active Site Complex Bambc of Benzoyl Coenzyme A Reductase As Isolated within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn707

b:58.3
occ:0.43
OE1 C:GLU257 2.0 0.7 1.0
OE1 C:GLU251 2.0 72.1 1.0
NE2 C:HIS255 2.1 0.5 1.0
ND1 C:HIS260 2.1 89.7 1.0
CD C:GLU257 2.5 0.7 1.0
OE2 C:GLU251 2.6 69.0 1.0
CD C:GLU251 2.6 69.9 1.0
OE2 C:GLU257 2.6 0.4 1.0
CE1 C:HIS255 2.8 0.0 1.0
CE1 C:HIS260 2.8 88.9 1.0
CD2 C:HIS255 3.2 0.8 1.0
CG C:HIS260 3.3 89.6 1.0
CG C:GLU257 3.8 0.1 1.0
CB C:HIS260 3.9 88.8 1.0
ND1 C:HIS255 4.0 0.1 1.0
NE2 C:HIS260 4.0 89.1 1.0
CG C:GLU251 4.1 68.5 1.0
CD1 C:LEU326 4.1 64.6 1.0
CG C:HIS255 4.2 0.7 1.0
CB C:GLU257 4.3 0.1 1.0
CD2 C:HIS260 4.3 89.8 1.0
CA C:GLU257 4.3 0.8 1.0
NZ C:LYS325 4.8 71.5 1.0
CG C:LEU326 4.9 64.4 1.0
CB C:GLU251 4.9 66.8 1.0
CD2 C:LEU326 5.0 64.7 1.0

Zinc binding site 4 out of 4 in 4z40

Go back to Zinc Binding Sites List in 4z40
Zinc binding site 4 out of 4 in the Active Site Complex Bambc of Benzoyl Coenzyme A Reductase As Isolated


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Active Site Complex Bambc of Benzoyl Coenzyme A Reductase As Isolated within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn707

b:60.2
occ:0.41
OE1 D:GLU257 2.0 97.2 1.0
OE1 D:GLU251 2.0 79.9 1.0
NE2 D:HIS255 2.1 0.8 1.0
ND1 D:HIS260 2.1 95.5 1.0
CD D:GLU257 2.5 99.2 1.0
OE2 D:GLU251 2.5 82.3 1.0
CD D:GLU251 2.5 80.4 1.0
OE2 D:GLU257 2.6 98.8 1.0
CE1 D:HIS255 2.8 0.0 1.0
CE1 D:HIS260 2.8 95.0 1.0
CD2 D:HIS255 3.3 0.8 1.0
CG D:HIS260 3.3 97.3 1.0
CG D:GLU257 3.8 0.8 1.0
CB D:HIS260 3.9 99.0 1.0
ND1 D:HIS255 4.0 0.9 1.0
CG D:GLU251 4.0 78.9 1.0
NE2 D:HIS260 4.0 96.1 1.0
CD1 D:LEU326 4.1 82.8 1.0
CG D:HIS255 4.2 0.3 1.0
CD2 D:HIS260 4.3 97.2 1.0
CB D:GLU257 4.3 0.8 1.0
CA D:GLU257 4.4 0.8 1.0
NZ D:LYS325 4.8 81.6 1.0
CG D:LEU326 4.9 79.7 1.0
CB D:GLU251 4.9 77.8 1.0
CD2 D:LEU326 4.9 80.5 1.0

Reference:

T.Weinert, S.G.Huwiler, J.W.Kung, S.Weidenweber, P.Hellwig, H.J.Stark, T.Biskup, S.Weber, J.J.Cotelesage, G.N.George, U.Ermler, M.Boll. Structural Basis of Enzymatic Benzene Ring Reduction. Nat.Chem.Biol. V. 11 586 2015.
ISSN: ESSN 1552-4469
PubMed: 26120796
DOI: 10.1038/NCHEMBIO.1849
Page generated: Wed Dec 16 05:58:46 2020

Last articles

Zn in 7RE3
Zn in 7RDX
Zn in 7RDZ
Zn in 7RWM
Zn in 7PGU
Zn in 7PGR
Zn in 7PGT
Zn in 7PGS
Zn in 7SQE
Zn in 7RWK
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy