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Structure of cntnw N149L in the intermediate 2 state

Analyse Structure of cntnw N149L in the intermediate 2 state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5L24
Type
protein
Length
1,227 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Nucleoside permease
UniProt
G4CRQ5
Ligands
6ZL
Pockets
20 · best druggability 0.87

Structure

x-ray diffraction · 3 distinct chains · 75% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANucleoside permeaseprotein42074% helix, 0% strandG4CRQ5
CNucleoside permeaseprotein39975% helix, 0% strandG4CRQ5
BNucleoside permeaseprotein40876% helix, 0% strandG4CRQ5

Ligands and binding sites

  • 6ZL · 2-{[(4-O-alpha-D-glucopyranosyl-beta-D-glucopyranosyl) oxy]methyl}-2-octyldecyl 4-O-alpha-D-glucopyranosyl-beta-D-glucopyranoside · ligand · 2 copies · chains B, A

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

Pockets

20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16760.870.9046empty
24950.780.8555empty
34500.740.8343empty
44050.720.8251empty
5500.670.9623empty

Interfaces

3 interfaces between chains.

  • A–C · 1354 Ų buried · 4 hydrogen bonds · protein-protein
  • C–B · 1331 Ų buried · 4 hydrogen bonds · protein-protein
  • A–B · 1306 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 5L24 · Structure of CNTnw N149L in the intermediate 2 state · the same entry in another collection · chain A against A, TM-score 1.00

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