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Magnesium in PDB 1aih: Catalytic Domain of Bacteriophage HP1 Integrase

Protein crystallography data

The structure of Catalytic Domain of Bacteriophage HP1 Integrase, PDB code: 1aih was solved by A.B.Hickman, S.Waninger, J.J.Scocca, F.Dyda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 42.400, 129.300, 234.200, 90.00, 90.00, 90.00
R / Rfree (%) 20.9 / 27.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Catalytic Domain of Bacteriophage HP1 Integrase (pdb code 1aih). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the Catalytic Domain of Bacteriophage HP1 Integrase, PDB code: 1aih:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5;

Magnesium binding site 1 out of 5 in 1aih

Go back to Magnesium Binding Sites List in 1aih
Magnesium binding site 1 out of 5 in the Catalytic Domain of Bacteriophage HP1 Integrase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Catalytic Domain of Bacteriophage HP1 Integrase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg100

b:53.7
occ:1.00
OE1 A:GLU263 4.0 49.8 1.0
O A:HOH2020 4.2 44.0 1.0
OE2 A:GLU263 4.6 75.8 1.0
CD A:GLU263 4.6 64.5 1.0
OE2 A:GLU260 4.7 0.1 1.0
OE1 A:GLU260 5.0 0.7 1.0

Magnesium binding site 2 out of 5 in 1aih

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Magnesium binding site 2 out of 5 in the Catalytic Domain of Bacteriophage HP1 Integrase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Catalytic Domain of Bacteriophage HP1 Integrase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg101

b:68.8
occ:1.00
OE1 B:GLU263 4.0 94.0 1.0
OE2 B:GLU260 4.1 92.7 1.0
CD B:GLU260 4.2 85.6 1.0
CG B:GLU260 4.2 63.5 1.0
OE2 B:GLU263 4.7 69.8 1.0
CD B:GLU263 4.8 77.9 1.0
OE1 B:GLU260 4.9 85.6 1.0

Magnesium binding site 3 out of 5 in 1aih

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Magnesium binding site 3 out of 5 in the Catalytic Domain of Bacteriophage HP1 Integrase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Catalytic Domain of Bacteriophage HP1 Integrase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg103

b:24.8
occ:1.00
OE2 B:GLU270 2.3 21.5 1.0
O B:HOH2065 2.4 32.9 1.0
OE1 C:GLU270 2.7 20.2 1.0
OE2 C:GLU270 2.7 25.7 1.0
CD C:GLU270 3.0 25.2 1.0
CD B:GLU270 3.4 31.6 1.0
OE1 B:GLU270 3.8 27.9 1.0
NH1 B:ARG181 4.4 55.3 1.0
NH2 C:ARG181 4.6 40.9 1.0
CG C:GLU270 4.6 17.4 1.0
NH1 C:ARG181 4.6 51.3 1.0
CG B:GLU270 4.7 34.5 1.0

Magnesium binding site 4 out of 5 in 1aih

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Magnesium binding site 4 out of 5 in the Catalytic Domain of Bacteriophage HP1 Integrase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Catalytic Domain of Bacteriophage HP1 Integrase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg104

b:48.7
occ:1.00
OE2 C:GLU263 2.6 46.7 1.0
OE1 C:GLU263 3.0 41.1 1.0
CD C:GLU263 3.1 45.4 1.0
CE2 C:TYR259 3.7 47.3 1.0
CD2 C:TYR259 3.9 43.5 1.0
OE1 C:GLU260 4.3 87.4 1.0
CG C:GLU263 4.6 29.6 1.0
CD C:GLU260 4.9 89.4 1.0
CZ C:TYR259 5.0 46.7 1.0

Magnesium binding site 5 out of 5 in 1aih

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Magnesium binding site 5 out of 5 in the Catalytic Domain of Bacteriophage HP1 Integrase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Catalytic Domain of Bacteriophage HP1 Integrase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg102

b:66.1
occ:1.00
CD D:GLU260 3.4 91.9 1.0
CG D:GLU260 3.5 71.5 1.0
OE1 D:GLU260 3.5 0.5 1.0
OE2 D:GLU260 3.9 89.6 1.0
OE1 D:GLU263 4.4 69.5 1.0
CB D:GLU260 4.8 47.7 1.0

Reference:

A.B.Hickman, S.Waninger, J.J.Scocca, F.Dyda. Molecular Organization in Site-Specific Recombination: the Catalytic Domain of Bacteriophage HP1 Integrase at 2.7 A Resolution. Cell(Cambridge,Mass.) V. 89 227 1997.
ISSN: ISSN 0092-8674
PubMed: 9108478
DOI: 10.1016/S0092-8674(00)80202-0
Page generated: Mon Dec 14 03:31:48 2020

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