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Crystal structure of StSPL (asymmetric form)

Analyse Crystal structure of StSPL (asymmetric form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3MAF
Type
protein
Length
836 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.971
Source
Symbiobacterium thermophilum
Molecule
sphingosine-1-phosphate lyase
EC
4.1.2.27
UniProt
Q67PY4
Ligands
CL, PO4
Pockets
10 · best druggability 0.77

Structure

x-ray diffraction · resolution 2.971 · 2 distinct chains · 44% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
Asphingosine-1-phosphate lyase (EC 4.1.2.27)protein44145% helix, 14% strandQ67PY4
Bsphingosine-1-phosphate lyase (EC 4.1.2.27)protein39543% helix, 15% strandQ67PY4

Ligands and binding sites

  • CL · Chloride ion · ion · chains A, B
  • PO4 · Phosphate ion · ion · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11150.770.9633empty
25250.750.8363CL
34180.730.8361PO4
42680.650.8239empty
51550.490.7823empty

Interfaces

1 interface between chains.

  • A–B · 5500 Ų buried · 57 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (cofactor).

Compared structures

  • 3MAF · Crystal structure of stspl (asymmetric form) · the same entry in another collection · chain A against A, TM-score 1.00

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