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Chlorine in PDB 3maf: Crystal Structure of Stspl (Asymmetric Form)

Enzymatic activity of Crystal Structure of Stspl (Asymmetric Form)

All present enzymatic activity of Crystal Structure of Stspl (Asymmetric Form):
4.1.2.27;

Protein crystallography data

The structure of Crystal Structure of Stspl (Asymmetric Form), PDB code: 3maf 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) 27.66 / 2.97
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 84.190, 84.900, 131.320, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 26.5

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Stspl (Asymmetric Form) (pdb code 3maf). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Stspl (Asymmetric Form), PDB code: 3maf:

Chlorine binding site 1 out of 1 in 3maf

Go back to Chlorine Binding Sites List in 3maf
Chlorine binding site 1 out of 1 in the Crystal Structure of Stspl (Asymmetric Form)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Stspl (Asymmetric Form) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl514

b:62.5
occ:1.00
NE2 B:HIS129 3.0 47.9 1.0
OH A:TYR105 3.5 27.7 1.0
N A:ALA103 3.8 45.0 1.0
CE1 A:TYR105 3.9 41.2 1.0
CE1 B:HIS129 4.0 52.5 1.0
CD2 B:HIS129 4.0 43.6 1.0
ND2 B:ASN126 4.1 38.0 1.0
CA A:ALA103 4.1 42.4 1.0
CZ A:TYR105 4.2 32.0 1.0
CE A:LLP311 4.6 26.2 1.0
O A:ALA103 4.6 44.0 1.0
CD2 B:LEU128 4.8 39.0 1.0
C A:ALA103 4.8 46.5 1.0
CB B:SER353 4.9 23.7 1.0
C A:GLY102 4.9 40.9 1.0
NZ A:LYS317 5.0 42.6 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: Sat Dec 12 09:54:42 2020

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