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Crystal structure of truncated flgd (monoclinic form) from the human pathogen helicobacter pylori (strain 26695)

Analyse Crystal structure of truncated flgd (monoclinic form) from the human pathogen… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5K5Y
Type
protein
Length
584 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Basal-body rod modification protein flgd
UniProt
O25565
Pockets
4 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 49% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DBasal-body rod modification protein flgdprotein1464% helix, 49% strandO25565

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16790.650.7457empty
25180.600.7442empty
3520.260.7413empty
4530.240.7211empty

Interfaces

3 interfaces between chains.

  • A–B · 498 Ų buried · 8 hydrogen bonds · protein-protein
  • B–C · 219 Ų buried · 0 hydrogen bonds · protein-protein
  • A–D · 92 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 5K5Y · Crystal structure of truncated FlgD (monoclinic form) from the human pathogen… · the same entry in another collection · chain A against A, TM-score 1.00

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