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Self-association of the H3 region of syntaxin 1A: implications for snare complex assembly

Analyse Self-association of the H3 region of syntaxin 1A: implications for snare… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1HVV
Type
protein
Length
256 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Syntaxin 1A
UniProt
P32851
Pockets
2 · best druggability 0.64

Structure

x-ray diffraction · 4 distinct chains · 91% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASyntaxin 1Aprotein6790% helix, 0% strandP32851
BSyntaxin 1Aprotein6295% helix, 0% strandP32851
CSyntaxin 1Aprotein6689% helix, 0% strandP32851
DSyntaxin 1Aprotein6192% helix, 0% strandP32851

Ligands and binding sites

  • TAR · D(-)-tartaric acid · additive · chains A, C

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11000.640.8920empty
21320.520.8019empty

Interfaces

6 interfaces between chains.

  • A–C · 1344 Ų buried · 3 hydrogen bonds · protein-protein
  • C–D · 1212 Ų buried · 10 hydrogen bonds · protein-protein
  • B–D · 1119 Ų buried · 7 hydrogen bonds · protein-protein
  • A–B · 1060 Ų buried · 4 hydrogen bonds · protein-protein
  • A–D · 429 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 1HVV · Self-association of the H3 region of syntaxin 1A: implications for snare complex assembly · the same entry in another collection · chain D against D, TM-score 1.00
  • P32851 · AlphaFold monomer V2.0 prediction for syntaxin-1A (P32851) · a predicted model of the same protein · chain B against A, TM-score 0.81

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