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Zinc in PDB 4g25: Crystal Structure of Proteinaceous Rnase P 1 (PRORP1) From A. Thaliana, Semet Substituted Form with Sr

Enzymatic activity of Crystal Structure of Proteinaceous Rnase P 1 (PRORP1) From A. Thaliana, Semet Substituted Form with Sr

All present enzymatic activity of Crystal Structure of Proteinaceous Rnase P 1 (PRORP1) From A. Thaliana, Semet Substituted Form with Sr:
3.1.26.5;

Protein crystallography data

The structure of Crystal Structure of Proteinaceous Rnase P 1 (PRORP1) From A. Thaliana, Semet Substituted Form with Sr, PDB code: 4g25 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) 33.50 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 41.844, 111.814, 140.226, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 23.4

Other elements in 4g25:

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

Strontium (Sr) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Proteinaceous Rnase P 1 (PRORP1) From A. Thaliana, Semet Substituted Form with Sr (pdb code 4g25). 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, Semet Substituted Form with Sr, PDB code: 4g25:

Zinc binding site 1 out of 1 in 4g25

Go back to Zinc Binding Sites List in 4g25
Zinc binding site 1 out of 1 in the Crystal Structure of Proteinaceous Rnase P 1 (PRORP1) From A. Thaliana, Semet Substituted Form with Sr


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, Semet Substituted Form with Sr within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1001

b:35.1
occ:1.00
 SG A:CYS347 2.0 40.2 1.0
NE2 A:HIS548 2.1 27.4 1.0
SG A:CYS565 2.3 36.7 1.0
SG A:CYS344 2.4 37.5 1.0
CD2 A:HIS548 2.9 26.9 1.0
CB A:CYS347 3.0 44.5 1.0
CB A:CYS344 3.1 36.4 1.0
CE1 A:HIS548 3.2 29.3 1.0
CB A:CYS565 3.4 31.1 1.0
N A:CYS347 3.6 45.3 1.0
CA A:CYS347 3.9 43.5 1.0
CG A:HIS548 4.2 28.4 1.0
ND1 A:HIS548 4.2 29.0 1.0
CA A:CYS565 4.3 28.9 1.0
CB A:CYS346 4.4 51.1 1.0
C A:CYS347 4.6 43.5 1.0
CA A:CYS344 4.6 35.5 1.0
C A:CYS346 4.7 46.7 1.0
CB A:GLU349 4.8 47.0 1.0
N A:LYS348 4.8 42.3 1.0
N A:GLU349 4.8 42.8 1.0
CG2 A:THR546 4.8 35.0 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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