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Chlorine in PDB 3zn4: VP16, A Capsid Protein of Bacteriophage P23-77 (VP16-Type-2)

Protein crystallography data

The structure of VP16, A Capsid Protein of Bacteriophage P23-77 (VP16-Type-2), PDB code: 3zn4 was solved by I.Rissanen, J.M.Grimes, A.Pawlowski, S.Mantynen, K.Harlos, J.K.H.Bamford, D.I.Stuart, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 17.79 / 1.26
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 76.600, 68.570, 31.580, 90.00, 96.44, 90.00
R / Rfree (%) 15.6 / 18.4

Chlorine Binding Sites:

The binding sites of Chlorine atom in the VP16, A Capsid Protein of Bacteriophage P23-77 (VP16-Type-2) (pdb code 3zn4). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the VP16, A Capsid Protein of Bacteriophage P23-77 (VP16-Type-2), PDB code: 3zn4:

Chlorine binding site 1 out of 1 in 3zn4

Go back to Chlorine Binding Sites List in 3zn4
Chlorine binding site 1 out of 1 in the VP16, A Capsid Protein of Bacteriophage P23-77 (VP16-Type-2)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of VP16, A Capsid Protein of Bacteriophage P23-77 (VP16-Type-2) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1169

b:18.4
occ:0.50
O A:HOH2055 2.7 22.0 0.5
NH2 A:ARG35 2.9 12.7 1.0
NE A:ARG35 3.1 15.4 1.0
CZ A:ARG35 3.5 16.0 1.0
CZ A:PHE89 3.6 11.8 1.0
CE2 A:TYR142 4.0 7.2 1.0
CE2 A:PHE89 4.1 13.2 1.0
CB A:ARG35 4.3 10.0 1.0
CD A:ARG35 4.4 12.6 1.0
CD2 A:TYR142 4.6 6.8 1.0
CZ A:TYR142 4.6 7.4 1.0
CE1 A:PHE89 4.7 11.3 1.0
OH A:TYR142 4.8 9.3 1.0
NH1 A:ARG35 4.8 14.6 1.0
O A:ARG35 4.8 11.9 1.0
O A:HOH2048 4.9 13.4 1.0
CG A:ARG35 4.9 10.0 1.0

Reference:

I.Rissanen, J.M.Grimes, A.Pawlowski, S.Mantynen, K.Harlos, J.K.H.Bamford, D.I.Stuart. Bacteriophage P23-77 Capsid Protein Structures Reveal the Archetype of An Ancient Branch From A Major Virus Lineage. Structure V. 21 718 2013.
ISSN: ISSN 0969-2126
PubMed: 23623731
DOI: 10.1016/J.STR.2013.02.026
Page generated: Sun Jul 21 08:11:33 2024

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