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An engineered streptavidin with improved affinity for the strep-tag II peptide : SAM2-strepii

Analyse An engineered streptavidin with improved affinity for the strep-tag II peptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1KL5
Type
protein
Length
502 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Streptavidin; Strep-tag II
UniProt
P22629
Pockets
6 · best druggability 0.61

Structure

x-ray diffraction · 6 distinct chains · 9% helix, 54% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AStreptavidinprotein1217% helix, 56% strandP22629
B, CStreptavidinprotein1208% helix, 56% strandP22629
DStreptavidinprotein1198% helix, 57% strandP22629
EStrep-tag IIprotein50% helix, 0% strand—
FStrep-tag IIprotein560% helix, 0% strand—
G, HStrep-tag IIprotein650% helix, 0% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12810.610.8032empty
22390.590.8031empty
32230.570.7937empty
41550.510.7935empty
51010.330.7222empty

Interfaces

14 interfaces between chains.

  • A–B · 1603 Ų buried · 21 hydrogen bonds · protein-protein
  • C–D · 1586 Ų buried · 20 hydrogen bonds · protein-protein
  • C–G · 453 Ų buried · 5 hydrogen bonds · protein-protein
  • D–H · 442 Ų buried · 4 hydrogen bonds · protein-protein
  • A–D · 430 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 1KL5 · an engineered streptavidin with improved affinity for the strep-tag II peptide… · the same entry in another collection · chain A against A, TM-score 1.00

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