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Structural consequences of a circular permutation on lipase B from candida antartica

Analyse Structural consequences of a circular permutation on lipase B from candida… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3ICV
Type
protein
Length
288 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Lipase B
EC
3.1.1.3
UniProt
P41365
Ligands
NAG
Pockets
1 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALipase B (EC 3.1.1.3)protein28833% helix, 17% strandP41365

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
  • BTB · 2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1570.330.7716empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 3ICV · Structural Consequences of a Circular Permutation on Lipase B from Candida Antartica · the same entry in another collection · chain A against A, TM-score 1.00
  • P41365 · AlphaFold monomer V2.0 prediction for lipase B (P41365) · a predicted model of the same protein · chain A against A, TM-score 0.92

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