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Core-streptavidin mutant W120F in complex with biotin at pH 7.5

Analyse Core-streptavidin mutant W120F in complex with biotin at pH 7.5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1SWP
Type
protein
Length
468 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Core-streptavidin
UniProt
P22629
Ligands
BTN, BTQ
Pockets
7 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 58% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DCore-streptavidinprotein1175% helix, 58% strandP22629

Ligands and binding sites

  • BTN · Biotin · ligand · 3 copies · chains A, D, B, C
  • BTQ · Epi-biotin · ligand · chains 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, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12880.680.8348BTN, BTQ
21450.590.8328BTN
32230.580.8034empty
41380.580.8325BTN
51730.570.8224empty

Interfaces

6 interfaces between chains.

  • C–D · 1623 Ų buried · 23 hydrogen bonds · protein-protein
  • A–B · 1587 Ų buried · 26 hydrogen bonds · protein-protein
  • B–C · 484 Ų buried · 2 hydrogen bonds · protein-protein
  • A–D · 482 Ų buried · 2 hydrogen bonds · protein-protein
  • B–D · 196 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 1SWP · Core-streptavidin mutant W120F in complex with biotin at pH 7.5 · the same entry in another collection · chain A against A, TM-score 1.00

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