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Circular permuted streptavidin E51/A46 in complex with biotin

Analyse Circular permuted streptavidin E51/A46 in complex with biotin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1SWG
Type
protein
Length
463 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Circularly permuted core-streptavidin E51/A46
UniProt
P22629
Ligands
BTN
Pockets
7 · best druggability 0.62

Structure

x-ray diffraction · 3 distinct chains · 8% helix, 60% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BCircularly permuted core-streptavidin E51/A46protein1125% helix, 61% strandP22629
CCircularly permuted core-streptavidin E51/A46protein12612% helix, 57% strandP22629
DCircularly permuted core-streptavidin E51/A46protein1135% helix, 61% strandP22629

Ligands and binding sites

  • BTN · Biotin · ligand · 4 copies · chains A, D, B, C

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

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13040.620.8045empty
21580.530.8026empty
31470.520.8024empty
41070.490.8121BTN
51130.470.7919BTN

Interfaces

6 interfaces between chains.

  • C–D · 1678 Ų buried · 30 hydrogen bonds · protein-protein
  • A–B · 1627 Ų buried · 31 hydrogen bonds · protein-protein
  • B–C · 436 Ų buried · 3 hydrogen bonds · protein-protein
  • A–D · 432 Ų buried · 2 hydrogen bonds · protein-protein
  • B–D · 219 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 1SWG · Circular permuted streptavidin E51/A46 in complex with biotin · the same entry in another collection · chain A against A, TM-score 1.00

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