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Zinc in PDB 6hih: Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath)

Protein crystallography data

The structure of Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath), PDB code: 6hih was solved by H.Adams, T.M.Chicano, M.A.Hough, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 61.20 / 1.60
Space group P 21 3
Cell size a, b, c (Å), α, β, γ (°) 105.960, 105.960, 105.960, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 20.2

Other elements in 6hih:

The structure of Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath) also contains other interesting chemical elements:

Iron (Fe) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath) (pdb code 6hih). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath), PDB code: 6hih:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 6hih

Go back to Zinc Binding Sites List in 6hih
Zinc binding site 1 out of 2 in the Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn202

b:21.2
occ:0.33
NE2 A:HIS71 2.1 21.3 1.0
O A:HOH344 2.2 27.4 1.0
CE1 A:HIS71 3.1 23.7 1.0
CD2 A:HIS71 3.1 24.5 1.0
OD1 A:ASN70 4.1 28.4 1.0
O B:HOH301 4.1 44.5 1.0
ND1 A:HIS71 4.2 25.4 1.0
CG A:HIS71 4.3 24.0 1.0

Zinc binding site 2 out of 2 in 6hih

Go back to Zinc Binding Sites List in 6hih
Zinc binding site 2 out of 2 in the Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn204

b:59.7
occ:0.80
OE2 B:GLU68 2.0 58.0 1.0
ND1 B:HIS71 2.5 43.5 1.0
O B:HOH377 2.5 50.9 0.8
CE1 B:HIS71 3.0 56.6 1.0
CD B:GLU68 3.2 39.7 1.0
O A:HOH305 3.7 40.5 1.0
CG B:HIS71 3.8 44.6 1.0
OE1 A:GLN23 3.8 40.6 1.0
OE1 B:GLU68 3.8 40.7 1.0
O A:HOH363 4.1 51.4 1.0
CA B:HIS71 4.2 36.6 1.0
CG B:GLU68 4.3 37.4 1.0
NE2 B:HIS71 4.3 55.6 1.0
CB B:HIS71 4.4 43.6 1.0
CD2 B:HIS71 4.7 50.7 1.0
CD A:GLN23 4.7 35.4 1.0
N B:HIS71 4.9 34.6 1.0

Reference:

H.R.Adams, C.Krewson, J.E.Vardanega, S.Fujii, T.Moreno, Y.Sambongi, D.Svistunenko, J.Paps, C.R.Andrew, M.A.Hough. One Fold, Two Functions: Cytochrome P460 and Cytochromec'-Beta From the Methanotrophmethylococcus Capsulatus(Bath). Chem Sci V. 10 3031 2019.
ISSN: ISSN 2041-6520
PubMed: 30996884
DOI: 10.1039/C8SC05210G
Page generated: Wed Dec 16 11:57:15 2020

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