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Sodium in PDB 3mbb: Crystal Structure of Stspl - Apo Form, After Treatment with Semicarbazide

Enzymatic activity of Crystal Structure of Stspl - Apo Form, After Treatment with Semicarbazide

All present enzymatic activity of Crystal Structure of Stspl - Apo Form, After Treatment with Semicarbazide:
4.1.2.27;

Protein crystallography data

The structure of Crystal Structure of Stspl - Apo Form, After Treatment with Semicarbazide, PDB code: 3mbb was solved by F.Bourquin, M.G.Grutter, G.Capitani, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.41 / 2.05
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 57.650, 126.990, 136.780, 90.00, 90.00, 90.00
R / Rfree (%) 18.1 / 21.8

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Stspl - Apo Form, After Treatment with Semicarbazide (pdb code 3mbb). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of Stspl - Apo Form, After Treatment with Semicarbazide, PDB code: 3mbb:

Sodium binding site 1 out of 1 in 3mbb

Go back to Sodium Binding Sites List in 3mbb
Sodium binding site 1 out of 1 in the Crystal Structure of Stspl - Apo Form, After Treatment with Semicarbazide


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Stspl - Apo Form, After Treatment with Semicarbazide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na517

b:22.8
occ:1.00
O A:ILE395 2.7 27.8 1.0
O A:LEU398 2.8 25.0 1.0
O A:ARG393 2.9 25.4 1.0
O A:HOH547 3.0 33.5 1.0
O A:VAL392 3.2 27.9 1.0
C A:ARG393 3.3 28.0 1.0
CA A:ARG393 3.6 27.6 1.0
C A:ILE395 3.6 24.9 1.0
C A:LEU398 3.8 30.7 1.0
N A:ILE395 4.0 26.1 1.0
C A:VAL392 4.1 26.1 1.0
N A:LEU398 4.2 25.0 1.0
N A:ALA394 4.3 22.6 1.0
N A:ARG393 4.3 23.6 1.0
CA A:ILE395 4.4 24.0 1.0
CA A:LEU398 4.4 24.2 1.0
C A:ALA394 4.5 31.1 1.0
N A:PRO396 4.5 25.4 1.0
CB A:LEU398 4.5 22.3 1.0
CA A:PRO396 4.6 22.8 1.0
N A:LYS399 4.8 24.5 1.0
N A:SER397 4.8 23.5 1.0
CB A:ARG393 4.8 28.3 1.0
CA A:ALA394 4.8 28.2 1.0
C A:PRO396 4.9 22.3 1.0
CA A:LYS399 4.9 25.1 1.0

Reference:

F.Bourquin, H.Riezman, G.Capitani, M.G.Grutter. Structure and Function of Sphingosine-1-Phosphate Lyase, A Key Enzyme of Sphingolipid Metabolism. Structure V. 18 1054 2010.
ISSN: ISSN 0969-2126
PubMed: 20696404
DOI: 10.1016/J.STR.2010.05.011
Page generated: Mon Oct 7 11:28:08 2024

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