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Calcium in PDB 2vbn: Molecular Basis of Human Xpc Gene Recognition and Cleavage By Engineered Homing Endonuclease Heterodimers

Protein crystallography data

The structure of Molecular Basis of Human Xpc Gene Recognition and Cleavage By Engineered Homing Endonuclease Heterodimers, PDB code: 2vbn was solved by P.Redondo, J.Prieto, I.G.Munoz, A.Alibes, F.Stricher, L.Serrano, S.Arnould, C.Perez, J.P.Cabaniols, P.Duchateau, F.Paques, F.J.Blanco, G.Montoya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.13 / 1.9
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 46.115, 67.992, 77.186, 90.00, 90.11, 90.00
R / Rfree (%) 14.1 / 22.3

Other elements in 2vbn:

The structure of Molecular Basis of Human Xpc Gene Recognition and Cleavage By Engineered Homing Endonuclease Heterodimers also contains other interesting chemical elements:

Magnesium (Mg) 3 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Molecular Basis of Human Xpc Gene Recognition and Cleavage By Engineered Homing Endonuclease Heterodimers (pdb code 2vbn). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Molecular Basis of Human Xpc Gene Recognition and Cleavage By Engineered Homing Endonuclease Heterodimers, PDB code: 2vbn:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 2vbn

Go back to Calcium Binding Sites List in 2vbn
Calcium binding site 1 out of 2 in the Molecular Basis of Human Xpc Gene Recognition and Cleavage By Engineered Homing Endonuclease Heterodimers


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Molecular Basis of Human Xpc Gene Recognition and Cleavage By Engineered Homing Endonuclease Heterodimers within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1155

b:16.0
occ:1.00
O A:HOH2099 2.0 33.6 1.0
O A:HOH2095 2.3 35.5 1.0
O A:ALA134 2.3 23.0 1.0
O A:HOH2100 2.4 22.9 1.0
O A:ASN136 2.5 23.3 1.0
O B:HOH2048 2.6 33.0 1.0
O A:HOH2096 2.7 39.3 1.0
C A:ALA134 3.5 23.5 1.0
C A:ASN136 3.7 21.2 1.0
O A:HOH2102 4.0 46.2 1.0
C A:LEU135 4.1 20.2 1.0
O A:LEU135 4.1 22.3 1.0
CA A:ALA134 4.3 23.2 1.0
CA A:ASP137 4.3 21.5 1.0
O A:ALA133 4.3 24.3 1.0
N A:ASN136 4.4 19.3 1.0
N A:ASP137 4.4 21.1 1.0
N A:LEU135 4.4 21.5 1.0
N A:SER138 4.5 20.1 1.0
O A:HOH2103 4.5 43.1 1.0
CA A:LEU135 4.5 22.8 1.0
NE2 B:GLN50 4.6 36.8 1.0
OD1 A:ASP137 4.7 25.8 1.0
O A:HOH2039 4.7 37.5 1.0
CA A:ASN136 4.7 19.9 1.0
C A:ASP137 4.9 21.5 1.0

Calcium binding site 2 out of 2 in 2vbn

Go back to Calcium Binding Sites List in 2vbn
Calcium binding site 2 out of 2 in the Molecular Basis of Human Xpc Gene Recognition and Cleavage By Engineered Homing Endonuclease Heterodimers


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Molecular Basis of Human Xpc Gene Recognition and Cleavage By Engineered Homing Endonuclease Heterodimers within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca1154

b:18.7
occ:1.00
O B:HOH2113 2.1 43.0 1.0
O B:HOH2109 2.2 32.4 1.0
O B:ALA134 2.3 25.9 1.0
O B:HOH2112 2.4 21.3 1.0
O B:ASN136 2.5 23.9 1.0
O B:HOH2115 2.5 27.3 1.0
O B:HOH2108 2.5 35.3 1.0
C B:ALA134 3.4 24.2 1.0
C B:ASN136 3.6 22.5 1.0
O B:LEU135 4.0 23.8 1.0
C B:LEU135 4.1 23.9 1.0
CA B:ASP137 4.2 20.3 1.0
O B:HOH2116 4.2 42.1 1.0
CA B:ALA134 4.2 24.2 1.0
O B:ALA133 4.3 22.7 1.0
N B:ASP137 4.4 20.9 1.0
O B:HOH2110 4.4 44.0 1.0
N B:LEU135 4.4 23.3 1.0
N B:SER138 4.4 21.5 1.0
N B:ASN136 4.5 23.7 1.0
CA B:LEU135 4.5 24.8 1.0
O B:HOH2042 4.6 34.4 1.0
CA B:ASN136 4.7 23.5 1.0
OD1 B:ASP137 4.7 23.1 1.0
NE2 A:GLN50 4.8 39.5 1.0
C B:ASP137 4.8 21.6 1.0
OE1 A:GLN50 5.0 43.5 1.0

Reference:

P.Redondo, J.Prieto, I.G.Munoz, A.Alibes, F.Stricher, L.Serrano, J.P.Cabaniols, F.Daboussi, S.Arnould, C.Perez, P.Duchateau, F.Paques, F.J.Blanco, G.Montoya. Molecular Basis of Xeroderma Pigmentosum Group C Dna Recognition By Engineered Meganucleases Nature V. 456 107 2008.
ISSN: ISSN 0028-0836
PubMed: 18987743
DOI: 10.1038/NATURE07343
Page generated: Tue Jul 8 08:32:52 2025

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