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Structure of savm-W120K, streptavidin mutant

Analyse Structure of savm-W120K, streptavidin mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1NQM
Type
protein
Length
476 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Streptavidin
UniProt
P22629
Ligands
BTN
Pockets
3 · best druggability 0.76

Structure

x-ray diffraction · 3 distinct chains · 5% helix, 56% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AStreptavidinprotein1185% helix, 57% strandP22629
B, CStreptavidinprotein1195% helix, 56% strandP22629
DStreptavidinprotein1205% helix, 56% strandP22629

Ligands and binding sites

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

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17030.760.8191BTN
25190.740.8273BTN
31770.540.8026empty

Interfaces

6 interfaces between chains.

  • A–C · 1541 Ų buried · 24 hydrogen bonds · protein-protein
  • B–D · 1523 Ų buried · 27 hydrogen bonds · protein-protein
  • A–B · 476 Ų buried · 2 hydrogen bonds · protein-protein
  • C–D · 459 Ų buried · 2 hydrogen bonds · protein-protein
  • B–C · 216 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 1NQM · Structure of Savm-W120K, streptavidin mutant · the same entry in another collection · chain A against A, TM-score 1.00

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