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Manganese in PDB 2x6n: Human Foamy Virus Integrase - Catalytic Core. Manganese- Bound Structure.

Protein crystallography data

The structure of Human Foamy Virus Integrase - Catalytic Core. Manganese- Bound Structure., PDB code: 2x6n was solved by S.Rety, O.Delelis, L.Rezabkova, B.Dubanchet, J.Silhan, A.Lewit-Bentley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.62 / 2.06
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 84.767, 89.232, 177.084, 90.00, 90.00, 90.00
R / Rfree (%) 22.574 / 27.004

Manganese Binding Sites:

The binding sites of Manganese atom in the Human Foamy Virus Integrase - Catalytic Core. Manganese- Bound Structure. (pdb code 2x6n). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 6 binding sites of Manganese where determined in the Human Foamy Virus Integrase - Catalytic Core. Manganese- Bound Structure., PDB code: 2x6n:
Jump to Manganese binding site number: 1; 2; 3; 4; 5; 6;

Manganese binding site 1 out of 6 in 2x6n

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Manganese binding site 1 out of 6 in the Human Foamy Virus Integrase - Catalytic Core. Manganese- Bound Structure.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Human Foamy Virus Integrase - Catalytic Core. Manganese- Bound Structure. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1197

b:31.2
occ:1.00
O A:HOH2082 2.0 22.4 1.0
O A:HOH2080 2.1 28.4 1.0
O A:HOH2079 2.2 26.6 1.0
OD2 A:ASP185 2.2 23.4 1.0
OD1 A:ASP128 2.2 21.3 1.0
O A:HOH2081 2.3 19.3 1.0
CG A:ASP185 3.1 24.2 1.0
CG A:ASP128 3.2 22.6 1.0
OD1 A:ASP185 3.4 24.8 1.0
OD2 A:ASP128 3.5 19.0 1.0
O A:HOH2006 4.0 18.1 1.0
O A:HOH2018 4.2 34.6 1.0
O A:TYR129 4.3 22.1 1.0
N A:TYR129 4.4 19.9 1.0
CB A:ASP185 4.5 23.6 1.0
CB A:ASP128 4.6 19.7 1.0
O A:HOH2039 4.9 54.2 1.0
CA A:ASP128 4.9 20.6 1.0

Manganese binding site 2 out of 6 in 2x6n

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Manganese binding site 2 out of 6 in the Human Foamy Virus Integrase - Catalytic Core. Manganese- Bound Structure.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Human Foamy Virus Integrase - Catalytic Core. Manganese- Bound Structure. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn1196

b:55.2
occ:1.00
OD2 B:ASP185 2.2 34.7 1.0
O B:HOH2075 2.3 41.5 1.0
OD1 B:ASP128 2.3 32.7 1.0
CG B:ASP185 3.2 34.5 1.0
CG B:ASP128 3.2 30.9 1.0
OD2 B:ASP128 3.4 33.9 1.0
OD1 B:ASP185 3.5 36.4 1.0
O B:HOH2009 4.1 35.2 1.0
O B:TYR129 4.2 28.1 1.0
O B:HOH2005 4.2 34.2 1.0
OH D:TYR263 4.2 39.0 1.0
O D:HOH2011 4.3 35.3 1.0
N B:TYR129 4.5 27.1 1.0
CB B:ASP185 4.6 31.2 1.0
CB B:ASP128 4.6 28.6 1.0
O B:HOH2006 4.7 52.6 1.0
CD D:LYS262 4.8 51.2 1.0

Manganese binding site 3 out of 6 in 2x6n

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Manganese binding site 3 out of 6 in the Human Foamy Virus Integrase - Catalytic Core. Manganese- Bound Structure.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Human Foamy Virus Integrase - Catalytic Core. Manganese- Bound Structure. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn1197

b:60.6
occ:1.00
O C:HOH2045 2.1 40.5 1.0
O C:HOH2044 2.1 43.2 1.0
O C:HOH2047 2.1 40.6 1.0
OD2 C:ASP185 2.2 50.1 1.0
OD1 C:ASP128 2.2 36.1 1.0
O C:HOH2046 2.9 42.4 1.0
CG C:ASP128 3.1 36.8 1.0
CG C:ASP185 3.1 49.6 1.0
OD2 C:ASP128 3.3 34.4 1.0
OD1 C:ASP185 3.4 49.6 1.0
O C:HOH2019 4.1 44.9 1.0
O C:TYR129 4.2 35.2 1.0
O C:HOH2006 4.2 46.0 1.0
N C:TYR129 4.4 34.2 1.0
CB C:ASP185 4.5 49.7 1.0
CB C:ASP128 4.5 36.8 1.0
CA C:ASP128 5.0 36.1 1.0

Manganese binding site 4 out of 6 in 2x6n

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Manganese binding site 4 out of 6 in the Human Foamy Virus Integrase - Catalytic Core. Manganese- Bound Structure.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Human Foamy Virus Integrase - Catalytic Core. Manganese- Bound Structure. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn1196

b:85.4
occ:1.00
OD2 D:ASP185 2.0 66.0 1.0
OD1 D:ASP128 2.3 60.8 1.0
OD2 D:ASP128 3.0 60.5 1.0
CG D:ASP128 3.0 59.3 1.0
CG D:ASP185 3.2 66.3 1.0
OD1 D:ASP185 3.9 66.8 1.0
O D:TYR129 4.3 59.2 1.0
CB D:ASP185 4.3 66.3 1.0
CB D:ASP128 4.5 57.6 1.0
N D:TYR129 4.7 57.3 1.0

Manganese binding site 5 out of 6 in 2x6n

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Manganese binding site 5 out of 6 in the Human Foamy Virus Integrase - Catalytic Core. Manganese- Bound Structure.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of Human Foamy Virus Integrase - Catalytic Core. Manganese- Bound Structure. within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mn1193

b:44.6
occ:1.00
O E:HOH2050 2.0 38.5 1.0
OD1 E:ASP128 2.2 29.3 1.0
O E:HOH2051 2.2 42.3 1.0
OD2 E:ASP185 2.2 29.3 1.0
O E:HOH2052 2.3 31.5 1.0
O E:HOH2004 2.4 30.1 1.0
CG E:ASP128 3.1 29.6 1.0
CG E:ASP185 3.2 28.2 1.0
OD2 E:ASP128 3.4 31.7 1.0
OD1 E:ASP185 3.5 31.1 1.0
O E:HOH2003 4.1 29.8 1.0
O E:TYR129 4.2 29.2 1.0
O E:HOH2007 4.4 33.6 1.0
N E:TYR129 4.5 27.6 1.0
CB E:ASP128 4.5 28.2 1.0
CB E:ASP185 4.6 26.0 1.0
CA E:ASP128 4.9 27.6 1.0

Manganese binding site 6 out of 6 in 2x6n

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Manganese binding site 6 out of 6 in the Human Foamy Virus Integrase - Catalytic Core. Manganese- Bound Structure.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 6 of Human Foamy Virus Integrase - Catalytic Core. Manganese- Bound Structure. within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mn1195

b:41.6
occ:1.00
O F:HOH2034 2.1 37.5 1.0
OD2 F:ASP185 2.1 32.0 1.0
O F:HOH2036 2.3 35.2 1.0
OD1 F:ASP128 2.3 30.4 1.0
O F:HOH2033 2.4 30.5 1.0
O F:HOH2035 2.5 33.4 1.0
CG F:ASP185 3.1 32.2 1.0
CG F:ASP128 3.2 30.7 1.0
OD1 F:ASP185 3.4 32.8 1.0
OD2 F:ASP128 3.5 30.2 1.0
O F:HOH2002 4.2 34.6 1.0
O F:TYR129 4.3 31.8 1.0
CB F:ASP185 4.5 31.4 1.0
O F:HOH2006 4.5 34.4 1.0
N F:TYR129 4.6 28.8 1.0
O F:HOH2019 4.6 41.2 1.0
CB F:ASP128 4.6 30.4 1.0

Reference:

S.Rety, L.Rezabkova, B.Dubanchet, J.Silhan, P.Legrand, A.Lewit-Bentley. Structural Studies of the Catalytic Core of the Primate Foamy Virus (Pfv-1) Integrase Acta Crystallogr.,Sect.F V. 66 881 2010.
ISSN: ISSN 1744-3091
PubMed: 20693659
DOI: 10.1107/S1744309110022852
Page generated: Sat Oct 5 15:25:26 2024

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