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Magnesium in PDB 2zl5: Atomic Resolution Structural Characterization of Recognition of Histo-Blood Group Antigen By Norwalk Virus

Protein crystallography data

The structure of Atomic Resolution Structural Characterization of Recognition of Histo-Blood Group Antigen By Norwalk Virus, PDB code: 2zl5 was solved by J.M.Choi, A.M.Huston, M.K.Estes, B.V.V.Prasad, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.10 / 1.47
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 83.517, 83.517, 163.368, 90.00, 90.00, 120.00
R / Rfree (%) 18.1 / 20

Other elements in 2zl5:

The structure of Atomic Resolution Structural Characterization of Recognition of Histo-Blood Group Antigen By Norwalk Virus also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Atomic Resolution Structural Characterization of Recognition of Histo-Blood Group Antigen By Norwalk Virus (pdb code 2zl5). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Atomic Resolution Structural Characterization of Recognition of Histo-Blood Group Antigen By Norwalk Virus, PDB code: 2zl5:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 2zl5

Go back to Magnesium Binding Sites List in 2zl5
Magnesium binding site 1 out of 2 in the Atomic Resolution Structural Characterization of Recognition of Histo-Blood Group Antigen By Norwalk Virus


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Atomic Resolution Structural Characterization of Recognition of Histo-Blood Group Antigen By Norwalk Virus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg522

b:20.7
occ:1.00
OH A:TYR441 2.6 12.9 1.0
O A:LEU236 2.8 11.4 1.0
O A:PRO234 2.9 11.9 1.0
N A:PHE501 3.2 12.3 1.0
CZ A:TYR441 3.5 11.5 1.0
CE1 A:TYR441 3.7 10.9 1.0
CA A:VAL500 3.7 12.4 1.0
CG1 A:VAL500 3.7 13.7 1.0
O A:PHE501 3.9 13.1 1.0
C A:VAL500 3.9 13.3 1.0
C A:LEU236 4.0 10.3 1.0
C A:PRO234 4.0 11.5 1.0
N A:LEU236 4.0 9.9 1.0
CA A:PHE501 4.1 12.5 1.0
CD2 A:LEU238 4.2 14.5 1.0
CB A:VAL500 4.2 12.1 1.0
CB A:PHE501 4.3 12.4 1.0
C A:PHE501 4.5 13.1 1.0
CA A:LEU236 4.6 10.5 1.0
CB A:PRO234 4.7 12.2 1.0
CG2 A:VAL500 4.7 13.2 1.0
CE2 A:TYR441 4.7 11.5 1.0
O A:GLY499 4.7 12.9 1.0
CA A:PRO234 4.8 11.6 1.0
CD2 A:PHE501 4.9 11.7 1.0
CD1 A:LEU241 4.9 10.3 1.0
N A:PRO234 4.9 11.5 1.0
CD1 A:TYR441 5.0 10.9 1.0
N A:ASN235 5.0 11.4 1.0
N A:VAL500 5.0 12.3 1.0

Magnesium binding site 2 out of 2 in 2zl5

Go back to Magnesium Binding Sites List in 2zl5
Magnesium binding site 2 out of 2 in the Atomic Resolution Structural Characterization of Recognition of Histo-Blood Group Antigen By Norwalk Virus


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Atomic Resolution Structural Characterization of Recognition of Histo-Blood Group Antigen By Norwalk Virus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1

b:21.1
occ:1.00
OH B:TYR441 2.7 13.4 1.0
O B:LEU236 2.8 11.3 1.0
O B:PRO234 2.9 11.8 1.0
N B:PHE501 3.2 12.3 1.0
CZ B:TYR441 3.6 11.8 1.0
CG1 B:VAL500 3.6 13.0 1.0
CE1 B:TYR441 3.7 10.8 1.0
CA B:VAL500 3.7 12.4 1.0
O B:PHE501 3.9 13.2 1.0
C B:VAL500 3.9 13.3 1.0
C B:LEU236 3.9 11.2 1.0
N B:LEU236 4.0 9.7 1.0
C B:PRO234 4.1 11.4 1.0
CA B:PHE501 4.1 12.4 1.0
CB B:VAL500 4.2 11.9 1.0
CB B:PHE501 4.2 12.9 1.0
CD2 B:LEU238 4.4 14.2 1.0
C B:PHE501 4.5 13.5 1.0
CA B:LEU236 4.6 10.8 1.0
CG2 B:VAL500 4.7 12.8 1.0
CB B:PRO234 4.7 11.3 1.0
CE2 B:TYR441 4.8 12.4 1.0
O B:GLY499 4.8 12.3 1.0
CA B:PRO234 4.9 11.4 1.0
CD1 B:LEU241 4.9 9.0 1.0
CD2 B:PHE501 4.9 11.8 1.0
N B:VAL500 5.0 12.1 1.0
N B:PRO234 5.0 11.0 1.0
N B:ASN235 5.0 11.0 1.0
CA B:ASN235 5.0 11.2 1.0

Reference:

J.M.Choi, A.M.Hutson, M.K.Estes, B.V.V.Prasad. Atomic Resolution Structural Characterization of Recognition of Histo-Blood Group Antigens By Norwalk Virus Proc.Natl.Acad.Sci.Usa V. 105 9175 2008.
ISSN: ISSN 0027-8424
PubMed: 18599458
DOI: 10.1073/PNAS.0803275105
Page generated: Mon Dec 14 07:50:37 2020

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