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Zinc in PDB 1nj6: Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus Bound to Alanine Sulfamoyl Adenylate

Enzymatic activity of Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus Bound to Alanine Sulfamoyl Adenylate

All present enzymatic activity of Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus Bound to Alanine Sulfamoyl Adenylate:
6.1.1.15;

Protein crystallography data

The structure of Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus Bound to Alanine Sulfamoyl Adenylate, PDB code: 1nj6 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) 29.16 / 2.85
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 143.539, 143.539, 164.178, 90.00, 90.00, 120.00
R / Rfree (%) 22.3 / 25.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus Bound to Alanine Sulfamoyl Adenylate (pdb code 1nj6). 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 Bound to Alanine Sulfamoyl Adenylate, PDB code: 1nj6:

Zinc binding site 1 out of 1 in 1nj6

Go back to Zinc Binding Sites List in 1nj6
Zinc binding site 1 out of 1 in the Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus Bound to Alanine Sulfamoyl Adenylate


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 Bound to Alanine Sulfamoyl Adenylate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn509

b:67.2
occ:1.00
SG A:CYS464 2.3 60.2 1.0
SG A:CYS441 2.3 74.9 1.0
SG A:CYS436 2.4 64.4 1.0
SG A:CYS467 2.5 74.9 1.0
CB A:CYS464 3.0 65.0 1.0
CB A:CYS436 3.0 64.8 1.0
CB A:CYS441 3.3 74.6 1.0
CB A:CYS467 3.7 72.9 1.0
N A:CYS436 3.8 62.6 1.0
N A:CYS467 3.9 71.0 1.0
CD1 A:TRP435 3.9 67.4 1.0
CA A:CYS436 4.0 65.4 1.0
NE1 A:TRP435 4.2 66.9 1.0
NH2 A:ARG469 4.3 81.9 1.0
CA A:CYS467 4.3 72.3 1.0
CA A:CYS464 4.5 67.4 1.0
CB A:ASN466 4.5 69.7 1.0
CA A:CYS441 4.8 75.1 1.0
C A:CYS436 4.8 67.9 1.0
N A:GLY437 4.8 70.0 1.0
NE A:ARG469 4.9 81.7 1.0
C A:ASN466 4.9 70.0 1.0
C A:CYS464 5.0 67.9 1.0
C A:TRP435 5.0 60.6 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: Fri Sep 25 22:44:33 2020
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