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Zinc in PDB 4cs8: Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer, Form 2

Protein crystallography data

The structure of Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer, Form 2, PDB code: 4cs8 was solved by C.Leyrat, M.Renner, K.Harlos, J.M.Grimes, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.75 / 2.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 49.980, 93.420, 85.210, 90.00, 95.44, 90.00
R / Rfree (%) 19.23 / 22.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer, Form 2 (pdb code 4cs8). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer, Form 2, PDB code: 4cs8:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 4cs8

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Zinc binding site 1 out of 4 in the Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer, Form 2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer, Form 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1171

b:49.5
occ:1.00
NE2 A:HIS25 2.0 47.9 1.0
SG A:CYS15 2.2 52.5 1.0
SG A:CYS21 2.2 61.8 1.0
SG A:CYS7 2.4 42.5 1.0
CE1 A:HIS25 2.9 48.5 1.0
CB A:CYS15 3.0 49.4 1.0
CD2 A:HIS25 3.1 48.1 1.0
CB A:CYS21 3.3 59.7 1.0
CB A:CYS7 3.3 39.1 1.0
ND1 A:HIS25 4.1 49.7 1.0
CG A:HIS25 4.1 47.6 1.0
CA A:CYS15 4.5 50.5 1.0
CD2 A:TYR9 4.6 41.2 1.0
CA A:CYS7 4.7 39.1 1.0
CA A:CYS21 4.7 61.2 1.0
CB A:TYR9 4.7 37.4 1.0
CB A:PHE23 4.8 56.6 1.0
O A:HOH2012 4.8 72.7 1.0

Zinc binding site 2 out of 4 in 4cs8

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Zinc binding site 2 out of 4 in the Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer, Form 2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer, Form 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1169

b:61.0
occ:1.00
NE2 B:HIS25 2.0 64.7 1.0
SG B:CYS15 2.2 62.7 1.0
SG B:CYS7 2.2 64.3 1.0
SG B:CYS21 2.3 80.5 1.0
CE1 B:HIS25 3.0 64.8 1.0
CD2 B:HIS25 3.0 64.4 1.0
CB B:CYS15 3.0 58.7 1.0
CB B:CYS21 3.1 77.4 1.0
CB B:CYS7 3.3 61.5 1.0
ND1 B:HIS25 4.1 65.1 1.0
CG B:HIS25 4.1 62.6 1.0
NE B:ARG17 4.2 95.5 1.0
CA B:CYS15 4.4 58.6 1.0
CA B:CYS21 4.6 78.3 1.0
CA B:CYS7 4.6 62.4 1.0
CD B:ARG17 4.6 87.3 1.0
CD1 B:TYR9 4.7 61.0 1.0
CB B:PHE23 4.7 75.3 1.0
CB B:TYR9 4.7 55.7 1.0

Zinc binding site 3 out of 4 in 4cs8

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Zinc binding site 3 out of 4 in the Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer, Form 2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer, Form 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn1173

b:51.3
occ:0.80
NE2 C:HIS25 2.0 55.2 1.0
SG C:CYS15 2.2 69.8 1.0
SG C:CYS21 2.3 73.3 1.0
SG C:CYS7 2.4 53.6 1.0
CE1 C:HIS25 2.9 55.4 1.0
CD2 C:HIS25 3.0 55.1 1.0
CB C:CYS15 3.1 65.5 1.0
CB C:CYS21 3.1 70.2 1.0
CB C:CYS7 3.2 49.7 1.0
O C:HOH2012 4.1 67.4 1.0
ND1 C:HIS25 4.1 56.0 1.0
CG C:HIS25 4.1 54.0 1.0
CA C:CYS15 4.5 65.3 1.0
CA C:CYS21 4.6 71.2 1.0
CA C:CYS7 4.6 50.0 1.0
CB C:PHE23 4.9 66.1 1.0
CB C:TYR9 4.9 57.7 1.0
CD2 C:TYR9 4.9 63.8 1.0
CB C:ARG17 5.0 80.4 1.0

Zinc binding site 4 out of 4 in 4cs8

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Zinc binding site 4 out of 4 in the Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer, Form 2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer, Form 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Zn1177

b:38.0
occ:1.00
NE2 E:HIS25 2.0 39.8 1.0
SG E:CYS15 2.2 39.4 1.0
SG E:CYS7 2.3 42.2 1.0
SG E:CYS21 2.3 38.5 1.0
CE1 E:HIS25 2.9 39.6 1.0
CB E:CYS15 3.1 36.3 1.0
CD2 E:HIS25 3.1 39.4 1.0
CB E:CYS21 3.2 36.1 1.0
CB E:CYS7 3.3 39.8 1.0
O E:HOH2010 3.8 36.7 1.0
ND1 E:HIS25 4.1 40.1 1.0
CG E:HIS25 4.2 38.2 1.0
CA E:CYS15 4.4 37.2 1.0
CA E:CYS7 4.6 41.4 1.0
CA E:CYS21 4.6 37.2 1.0
CD2 E:TYR9 4.7 44.9 1.0
CB E:PHE23 4.8 44.6 1.0
CB E:ARG17 4.9 40.1 1.0
CB E:TYR9 4.9 40.9 1.0

Reference:

C.Leyrat, M.Renner, K.Harlos, J.T.Huiskonen, J.M.Grimes. Drastic Changes in Conformational Dynamics of the Antiterminator M2-1 Regulate Transcription Efficiency in Pneumovirinae. Elife V. 3 02674 2014.
ISSN: ISSN 2050-084X
PubMed: 24842877
DOI: 10.7554/ELIFE.02674
Page generated: Sat Oct 26 21:00:39 2024

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