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Crystal structure of the outer membrane channel dcap of acinetobacter baumannii

Analyse Crystal structure of the outer membrane channel dcap of acinetobacter baumannii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6EUS
Type
protein
Length
2,076 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Dcap-like protein
UniProt
A0A0B9X9I7
Pockets
16 · best druggability 0.88

Structure

x-ray diffraction · 1 distinct chain · 1% helix, 61% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, FDcap-like proteinprotein3461% helix, 61% strandA0A0B9X9I7

Pockets

16 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13010.880.9829empty
23000.870.9730empty
38720.750.79107empty
410410.740.7794empty
510700.710.76105empty

Interfaces

7 interfaces between chains.

  • D–E · 1625 Ų buried · 16 hydrogen bonds · protein-protein
  • D–F · 1611 Ų buried · 16 hydrogen bonds · protein-protein
  • B–C · 1605 Ų buried · 17 hydrogen bonds · protein-protein
  • A–B · 1587 Ų buried · 16 hydrogen bonds · protein-protein
  • A–C · 1575 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 24 modified (engineered).

Compared structures

  • 6EUS · Crystal structure of the outer membrane channel DcaP of Acinetobacter baumannii · the same entry in another collection · chain B against B, TM-score 1.00

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