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Mutant a. fulgidus lipase S136A complexed with fatty acid fragment

Analyse Mutant a. fulgidus lipase S136A complexed with fatty acid fragment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2ZYH
Type
protein
Length
912 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Lipase, putative
EC
3.1.1.3
UniProt
O28511
Ligands
R16, CA
Pockets
7 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BLipase, putative (EC 3.1.1.3)protein45626% helix, 29% strandO28511

Ligands and binding sites

  • R16 · Hexadecane · ligand · 2 copies · chains A, B
  • CA · Calcium ion · metal · 2 copies · chains A, B

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

Pockets

7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16290.870.9196R16
27400.830.8694R16
35160.690.7969empty
42170.640.8325empty
51980.630.8325empty

Interfaces

1 interface between chains.

  • A–B · 647 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 2ZYH · mutant A. Fulgidus lipase S136A complexed with fatty acid fragment · the same entry in another collection · chain A against A, TM-score 1.00

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