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Zinc in PDB 4g24: Crystal Structure of Proteinaceous Rnase P 1 (PRORP1) From A. Thaliana with Mn

Enzymatic activity of Crystal Structure of Proteinaceous Rnase P 1 (PRORP1) From A. Thaliana with Mn

All present enzymatic activity of Crystal Structure of Proteinaceous Rnase P 1 (PRORP1) From A. Thaliana with Mn:
3.1.26.5;

Protein crystallography data

The structure of Crystal Structure of Proteinaceous Rnase P 1 (PRORP1) From A. Thaliana with Mn, PDB code: 4g24 was solved by M.Koutmos, M.J.Howard, C.A.Fierke, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.19 / 1.95
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 41.750, 112.475, 138.762, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 22.7

Other elements in 4g24:

The structure of Crystal Structure of Proteinaceous Rnase P 1 (PRORP1) From A. Thaliana with Mn also contains other interesting chemical elements:

Manganese (Mn) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Proteinaceous Rnase P 1 (PRORP1) From A. Thaliana with Mn (pdb code 4g24). 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 Proteinaceous Rnase P 1 (PRORP1) From A. Thaliana with Mn, PDB code: 4g24:

Zinc binding site 1 out of 1 in 4g24

Go back to Zinc Binding Sites List in 4g24
Zinc binding site 1 out of 1 in the Crystal Structure of Proteinaceous Rnase P 1 (PRORP1) From A. Thaliana with Mn


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 Proteinaceous Rnase P 1 (PRORP1) From A. Thaliana with Mn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1001

b:41.9
occ:1.00
SG A:CYS347 1.9 46.8 1.0
NE2 A:HIS548 2.2 33.7 1.0
SG A:CYS565 2.3 40.8 1.0
SG A:CYS344 2.4 42.0 1.0
CD2 A:HIS548 2.9 32.0 1.0
CB A:CYS344 3.1 40.2 1.0
CB A:CYS347 3.1 48.2 1.0
CE1 A:HIS548 3.3 32.9 1.0
CB A:CYS565 3.3 36.2 1.0
N A:CYS347 3.6 46.5 1.0
CA A:CYS347 3.9 45.2 1.0
CG A:HIS548 4.2 32.4 1.0
CA A:CYS565 4.3 34.8 1.0
ND1 A:HIS548 4.3 36.7 1.0
CB A:CYS346 4.5 51.0 1.0
CA A:CYS344 4.6 37.0 1.0
CB A:GLU349 4.6 50.6 1.0
C A:CYS347 4.6 46.2 1.0
C A:CYS346 4.7 49.0 1.0
N A:LYS348 4.8 48.5 1.0
O A:HOH1339 4.8 60.4 1.0
N A:GLU349 4.9 47.5 1.0
CG2 A:THR546 5.0 38.7 1.0

Reference:

M.J.Howard, W.H.Lim, C.A.Fierke, M.Koutmos. Mitochondrial Ribonuclease P Structure Provides Insight Into the Evolution of Catalytic Strategies For Precursor-Trna 5' Processing. Proc.Natl.Acad.Sci.Usa V. 109 16149 2012.
ISSN: ISSN 0027-8424
PubMed: 22991464
DOI: 10.1073/PNAS.1209062109
Page generated: Sat Oct 26 23:05:05 2024

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