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Zinc in PDB 1nj2: Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus

Enzymatic activity of Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus

All present enzymatic activity of Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus:
6.1.1.15;

Protein crystallography data

The structure of Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus, PDB code: 1nj2 was solved by S.Kamtekar, W.D.Kennedy, J.Wang, C.Stathopoulos, D.Soll, T.A.Steitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.95 / 3.11
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 145.077, 145.077, 170.359, 90.00, 90.00, 120.00
R / Rfree (%) 23.9 / 27.3

Other elements in 1nj2:

The structure of Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus (pdb code 1nj2). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus, PDB code: 1nj2:

Zinc binding site 1 out of 1 in 1nj2

Go back to Zinc Binding Sites List in 1nj2
Zinc binding site 1 out of 1 in the Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus


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 Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn495

b:70.6
occ:1.00
 SG A:CYS441 2.3 70.4 1.0
SG A:CYS464 2.4 75.0 1.0
SG A:CYS436 2.6 64.6 1.0
SG A:CYS467 2.6 87.0 1.0
CB A:CYS436 2.9 72.0 1.0
CB A:CYS464 3.0 77.4 1.0
CB A:CYS441 3.4 75.5 1.0
CB A:CYS467 3.5 85.7 1.0
N A:CYS436 3.6 74.7 1.0
N A:CYS467 3.8 83.2 1.0
CA A:CYS436 3.9 74.3 1.0
CD1 A:TRP435 3.9 80.4 1.0
CA A:CYS467 4.2 84.0 1.0
NE1 A:TRP435 4.4 80.6 1.0
CA A:CYS464 4.5 79.6 1.0
NH2 A:ARG469 4.6 95.8 1.0
N A:GLY437 4.8 79.2 1.0
CB A:ASN466 4.8 84.5 1.0
C A:TRP435 4.8 74.6 1.0
C A:CYS436 4.8 76.1 1.0
CA A:CYS441 4.8 77.0 1.0
C A:CYS467 4.9 84.2 1.0
C A:ASN466 4.9 83.0 1.0

Reference:

S.Kamtekar, W.D.Kennedy, J.Wang, C.Stathopoulos, D.Soll, T.A.Steitz. The Structural Basis of Cysteine Aminoacylation of Trnapro By Prolyl-Trna Synthetases Proc.Natl.Acad.Sci.Usa V. 100 1673 2003.
ISSN: ISSN 0027-8424
PubMed: 12578991
DOI: 10.1073/PNAS.0437911100
Page generated: Wed Oct 16 17:16:08 2024

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