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Apo-acp from helicobacter pylori

Analyse Apo-acp from helicobacter pylori in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5H9G
Type
protein
Length
161 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Acyl carrier protein
UniProt
B6JLE2

Structure

x-ray diffraction · 2 distinct chains · 61% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAcyl carrier proteinprotein8162% helix, 2% strandB6JLE2
BAcyl carrier proteinprotein8061% helix, 3% strandB6JLE2

Interfaces

1 interface between chains.

  • A–B · 397 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 5H9G · apo-ACP from Helicobacter pylori · the same entry in another collection · chain A against A, TM-score 1.00
  • B6JLE2 · AlphaFold monomer V2.0 prediction for acyl carrier protein (B6JLE2) · a predicted model of the same protein · chain B against A, TM-score 0.90

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