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Structure of the E. COLI chaperone papd in complex with the pilin domain of the papgii adhesin

Analyse Structure of the E. COLI chaperone papd in complex with the pilin domain of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3ME0
Type
protein
Length
344 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Chaperone protein papd; Papg protein
UniProt
P15319, Q8FDY8
Pockets
3 · best druggability 0.51

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AChaperone protein papdprotein2168% helix, 51% strandP15319
BPapg proteinprotein1280% helix, 52% strandQ8FDY8

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12330.510.7530empty
2950.350.7418empty
3630.280.7416empty

Interfaces

1 interface between chains.

  • A–B · 1904 Ų buried · 31 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 modified, 2 disulfide (engineered, disulfide).

Compared structures

  • 3ME0 · Structure of the E. coli chaperone PAPD in complex with the pilin domain of the PapGII… · the same entry in another collection · chain A against A, TM-score 1.00
  • P15319 · AlphaFold monomer V2.0 prediction for chaperone protein papd (P15319) · a predicted model of the same protein · chain A against A, TM-score 1.00

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