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Zinc in PDB 1li7: Crystal Structure of Cysteinyl-Trna Synthetase with Cysteine Substrate Bound

Enzymatic activity of Crystal Structure of Cysteinyl-Trna Synthetase with Cysteine Substrate Bound

All present enzymatic activity of Crystal Structure of Cysteinyl-Trna Synthetase with Cysteine Substrate Bound:
6.1.1.16;

Protein crystallography data

The structure of Crystal Structure of Cysteinyl-Trna Synthetase with Cysteine Substrate Bound, PDB code: 1li7 was solved by K.J.Newberry, Y.-M.Hou, J.J.Perona, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.95 / 2.60
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 118.980, 118.980, 143.840, 90.00, 90.00, 90.00
R / Rfree (%) 25 / 29

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Cysteinyl-Trna Synthetase with Cysteine Substrate Bound (pdb code 1li7). 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 with Cysteine Substrate Bound, PDB code: 1li7:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1li7

Go back to Zinc Binding Sites List in 1li7
Zinc binding site 1 out of 2 in the Crystal Structure of Cysteinyl-Trna Synthetase with Cysteine Substrate Bound


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 with Cysteine Substrate Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn963

b:41.9
occ:1.00
NE2 A:HIS234 1.9 31.9 1.0
SG A:CYS209 2.1 33.0 1.0
SG A:CYS28 2.4 33.8 1.0
SG A:CYS1000 2.6 42.0 1.0
CD2 A:HIS234 2.8 29.7 1.0
CE1 A:HIS234 3.0 28.9 1.0
OE2 A:GLU238 3.1 32.8 1.0
CB A:CYS28 3.2 33.8 1.0
CB A:CYS209 3.2 34.3 1.0
CB A:CYS1000 3.7 46.5 1.0
CG A:HIS234 4.0 29.6 1.0
ND1 A:HIS234 4.1 28.6 1.0
CD A:GLU238 4.1 35.6 1.0
CA A:CYS28 4.2 34.1 1.0
CE2 A:TYR26 4.5 29.5 1.0
CE1 A:HIS235 4.5 28.2 1.0
OH A:TYR26 4.6 28.0 1.0
CA A:CYS209 4.6 36.7 1.0
NE1 A:TRP205 4.7 48.7 1.0
OD1 A:ASN66 4.7 32.9 1.0
OE1 A:GLU238 4.7 34.6 1.0
ND1 A:HIS235 4.8 29.5 1.0
NE2 A:HIS224 4.9 26.1 1.0
CD1 A:LEU230 4.9 25.9 1.0
N A:CYS209 4.9 37.9 1.0
ND2 A:ASN66 5.0 32.4 1.0

Zinc binding site 2 out of 2 in 1li7

Go back to Zinc Binding Sites List in 1li7
Zinc binding site 2 out of 2 in the Crystal Structure of Cysteinyl-Trna Synthetase with Cysteine Substrate Bound


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 with Cysteine Substrate Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn964

b:53.8
occ:1.00
NE2 B:HIS234 1.8 36.4 1.0
SG B:CYS209 2.1 41.8 1.0
SG B:CYS1001 2.4 49.1 1.0
SG B:CYS28 2.5 32.4 1.0
CE1 B:HIS234 2.6 35.2 1.0
OE2 B:GLU238 2.8 34.5 1.0
CD2 B:HIS234 2.8 36.4 1.0
CB B:CYS209 2.9 41.3 1.0
CD B:GLU238 3.6 36.4 1.0
ND1 B:HIS234 3.7 35.2 1.0
CB B:CYS28 3.8 28.9 1.0
CG B:HIS234 3.8 36.5 1.0
CB B:CYS1001 4.0 53.0 1.0
OE1 B:GLU238 4.3 37.6 1.0
CA B:CYS209 4.3 42.7 1.0
CG B:GLU238 4.5 33.9 1.0
OH B:TYR26 4.5 33.0 1.0
CE2 B:TYR26 4.6 34.0 1.0
CA B:CYS28 4.6 31.0 1.0
CE1 B:HIS235 4.8 35.7 1.0
NE2 B:HIS224 4.8 25.8 1.0
N B:CYS209 4.8 43.8 1.0
OD1 B:ASN66 4.8 41.4 1.0
ND1 B:HIS235 4.8 35.8 1.0
NE1 B:TRP205 4.9 57.0 1.0
CA B:CYS1001 5.0 54.7 1.0

Reference:

K.J.Newberry, Y.-M.Hou, J.J.Perona. Structural Origins of Amino Acid Selection Without Editing By Cysteinyl-Trna Synthetase Embo J. V. 21 2778 2002.
ISSN: ISSN 0261-4189
PubMed: 12032090
DOI: 10.1093/EMBOJ/21.11.2778
Page generated: Wed Dec 16 02:56:21 2020

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