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Crystal structure of escherichia COLI bamd

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

PDB
3Q5M
Type
protein
Length
210 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
UPF0169 lipoprotein yfio
UniProt
P0AC02
Ligands
IOD
Pockets
1 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 75% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUPF0169 lipoprotein yfioprotein21075% helix, 0% strandP0AC02

Ligands and binding sites

  • IOD · Iodide ion · ion · 7 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1510.360.7919IOD

Compared structures

  • 3Q5M · Crystal structure of Escherichia coli BamD · 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 0.93

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