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Zinc in PDB 9b4r: Crystal Structure of Mras Bound to Gmppnp

Enzymatic activity of Crystal Structure of Mras Bound to Gmppnp

All present enzymatic activity of Crystal Structure of Mras Bound to Gmppnp:
3.6.5.2;

Protein crystallography data

The structure of Crystal Structure of Mras Bound to Gmppnp, PDB code: 9b4r was solved by D.J.Czyzyk, D.K.Simanshu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.54 / 2.10
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 65.481, 65.481, 107.806, 90, 90, 90
R / Rfree (%) 19.9 / 25

Other elements in 9b4r:

The structure of Crystal Structure of Mras Bound to Gmppnp also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Mras Bound to Gmppnp (pdb code 9b4r). 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 Mras Bound to Gmppnp, PDB code: 9b4r:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 9b4r

Go back to Zinc Binding Sites List in 9b4r
Zinc binding site 1 out of 2 in the Crystal Structure of Mras Bound to Gmppnp


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 Mras Bound to Gmppnp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn203

b:51.0
occ:1.00
NE2 A:HIS132 2.0 48.4 1.0
O A:HOH417 2.2 51.6 1.0
CD2 A:HIS132 3.0 47.5 1.0
CE1 A:HIS132 3.0 47.1 1.0
CG A:HIS132 4.1 45.7 1.0
ND1 A:HIS132 4.1 45.4 1.0

Zinc binding site 2 out of 2 in 9b4r

Go back to Zinc Binding Sites List in 9b4r
Zinc binding site 2 out of 2 in the Crystal Structure of Mras Bound to Gmppnp


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 Mras Bound to Gmppnp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn204

b:38.3
occ:1.00
ND1 A:HIS107 2.0 31.6 1.0
ND1 A:HIS148 2.2 32.1 1.0
O A:HOH419 2.2 30.4 1.0
CE1 A:HIS107 2.8 32.4 1.0
CE1 A:HIS148 3.1 34.1 1.0
CG A:HIS107 3.1 37.6 1.0
CG A:HIS148 3.2 34.2 1.0
CB A:HIS148 3.6 33.5 1.0
CB A:HIS107 3.6 31.3 1.0
CA A:HIS148 4.0 34.4 1.0
NE2 A:HIS107 4.0 30.5 1.0
CD2 A:HIS107 4.2 34.4 1.0
NE2 A:HIS148 4.2 42.1 1.0
CD2 A:HIS148 4.3 32.5 1.0
CD1 A:LEU111 4.6 34.5 1.0
O A:HIS148 4.7 29.9 1.0
C A:HIS107 4.7 26.8 1.0
N A:GLN108 4.7 28.7 1.0
CA A:HIS107 4.8 33.0 1.0
C A:HIS148 4.9 33.0 1.0
O A:HOH407 5.0 50.4 1.0

Reference:

D.Czyzyk, W.Yan, S.Messing, W.Gillette, T.Tsuji, M.Yamaguchi, S.Furuzono, D.M.Turner, D.Esposito, D.V.Nissley, F.Mccormick, D.K.Simanshu. Structural Insights Into Isoform-Specific Ras-PI3K Alpha Interactions and the Role of Ras in PI3K Alpha Activation. Nat Commun V. 16 525 2025.
ISSN: ESSN 2041-1723
PubMed: 39788953
DOI: 10.1038/S41467-024-55766-X
Page generated: Sun Feb 9 01:00:26 2025

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