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Zinc in PDB 3sp1: Crystal Structure of Cysteinyl-Trna Synthetase (Cyss) From Borrelia Burgdorferi

Enzymatic activity of Crystal Structure of Cysteinyl-Trna Synthetase (Cyss) From Borrelia Burgdorferi

All present enzymatic activity of Crystal Structure of Cysteinyl-Trna Synthetase (Cyss) From Borrelia Burgdorferi:
6.1.1.16;

Protein crystallography data

The structure of Crystal Structure of Cysteinyl-Trna Synthetase (Cyss) From Borrelia Burgdorferi, PDB code: 3sp1 was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.55
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 62.620, 49.890, 179.630, 90.00, 93.18, 90.00
R / Rfree (%) 22.4 / 27.4

Other elements in 3sp1:

The structure of Crystal Structure of Cysteinyl-Trna Synthetase (Cyss) From Borrelia Burgdorferi also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Cysteinyl-Trna Synthetase (Cyss) From Borrelia Burgdorferi (pdb code 3sp1). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Cysteinyl-Trna Synthetase (Cyss) From Borrelia Burgdorferi, PDB code: 3sp1:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 3sp1

Go back to Zinc Binding Sites List in 3sp1
Zinc binding site 1 out of 2 in the Crystal Structure of Cysteinyl-Trna Synthetase (Cyss) From Borrelia Burgdorferi


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 Cysteinyl-Trna Synthetase (Cyss) From Borrelia Burgdorferi within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn481

b:32.1
occ:1.00
O A:HOH525 2.0 22.1 1.0
NE2 A:HIS246 2.1 26.2 1.0
SG A:CYS221 2.2 24.1 1.0
SG A:CYS27 2.5 28.2 1.0
CB A:CYS27 3.0 24.4 1.0
CD2 A:HIS246 3.1 26.1 1.0
CE1 A:HIS246 3.2 26.3 1.0
OE2 A:GLU250 3.2 22.6 1.0
CB A:CYS221 3.3 22.1 1.0
CA A:CYS27 3.8 23.0 1.0
CD A:GLU250 4.2 23.5 1.0
CG A:HIS246 4.3 26.5 1.0
ND1 A:HIS246 4.3 27.1 1.0
OD1 A:ASN65 4.3 24.4 1.0
CE2 A:TYR25 4.5 22.2 1.0
CE3 A:TRP217 4.6 29.0 1.0
CA A:CYS221 4.6 21.3 1.0
N A:CYS27 4.8 21.9 1.0
OH A:TYR25 4.8 22.7 1.0
CZ3 A:TRP217 4.9 30.0 1.0
CE1 A:HIS236 4.9 16.9 1.0
OE1 A:GLU250 4.9 23.8 1.0
CG A:ASN65 5.0 23.7 1.0
NE2 A:HIS247 5.0 29.0 1.0
C A:CYS27 5.0 22.8 1.0

Zinc binding site 2 out of 2 in 3sp1

Go back to Zinc Binding Sites List in 3sp1
Zinc binding site 2 out of 2 in the Crystal Structure of Cysteinyl-Trna Synthetase (Cyss) From Borrelia Burgdorferi


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 Cysteinyl-Trna Synthetase (Cyss) From Borrelia Burgdorferi within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn481

b:30.8
occ:1.00
NE2 B:HIS246 2.2 29.4 1.0
SG B:CYS27 2.3 29.1 1.0
O B:HOH512 2.3 35.1 1.0
SG B:CYS221 2.5 19.9 1.0
CB B:CYS27 3.0 24.7 1.0
CD2 B:HIS246 3.1 29.8 1.0
CE1 B:HIS246 3.2 30.7 1.0
CB B:CYS221 3.4 20.2 1.0
OE2 B:GLU250 3.5 23.5 1.0
CA B:CYS27 3.8 22.8 1.0
CG B:HIS246 4.3 31.1 1.0
ND1 B:HIS246 4.3 32.4 1.0
CD B:GLU250 4.3 23.0 1.0
OD1 B:ASN65 4.3 22.7 1.0
CE3 B:TRP217 4.5 30.7 1.0
CZ3 B:TRP217 4.6 31.9 1.0
NE2 B:HIS247 4.7 29.8 1.0
OE1 B:GLU250 4.7 22.8 1.0
N B:CYS27 4.7 21.4 1.0
ND2 B:ASN65 4.8 23.9 1.0
CG B:ASN65 4.8 23.0 1.0
CA B:CYS221 4.8 20.3 1.0
CE2 B:TYR25 4.8 21.2 1.0
CD2 B:HIS247 4.9 28.9 1.0
O B:TRP217 4.9 22.6 1.0
C B:CYS27 5.0 22.2 1.0
CE1 B:HIS236 5.0 19.0 1.0
CE1 B:HIS242 5.0 28.3 1.0

Reference:

S.O.Moen, T.E.Edwards, D.M.Dranow, M.C.Clifton, B.Sankaran, W.C.Van Voorhis, A.Sharma, C.Manoil, B.L.Staker, P.J.Myler, D.D.Lorimer. Ligand Co-Crystallization of Aminoacyl-Trna Synthetases From Infectious Disease Organisms. Sci Rep V. 7 223 2017.
ISSN: ESSN 2045-2322
PubMed: 28303005
DOI: 10.1038/S41598-017-00367-6
Page generated: Wed Dec 16 04:50:43 2020

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