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Structure of bamd from E. COLI

Analyse Structure of bamd from E. COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2YHC
Type
protein
Length
209 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
UPF0169 lipoprotein yfio
UniProt
P0AC02
Ligands
URE
Pockets
3 · best druggability 0.39

Structure

x-ray diffraction · 1 distinct chain · 76% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUPF0169 lipoprotein yfioprotein20976% helix, 0% strandP0AC02

Ligands and binding sites

  • URE · Urea · ligand · chains A

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1580.390.8012empty
2540.330.7815empty
3580.270.7313empty

Compared structures

  • 2YHC · Structure of BamD from E. coli · the same entry in another collection · chain A against A, TM-score 1.00
  • P0AC02 · AlphaFold monomer V2.0 prediction for outer membrane protein assembly factor bamd (P0AC02) · a predicted model of the same protein · chain A against A, TM-score 0.87

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