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Crystal structure of ripc from yersinia pestis

Analyse Crystal structure of ripc from yersinia pestis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3QLL
Type
protein
Length
645 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Citrate lyase
UniProt
Q9ZC38
Pockets
6 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CCitrate lyaseprotein21547% helix, 18% strandQ9ZC38

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12220.660.8427empty
21870.660.8534empty
31790.510.7824empty
41710.470.7628empty
51470.450.7628empty

Interfaces

3 interfaces between chains.

  • A–B · 514 Ų buried · 1 hydrogen bond · protein-protein
  • B–C · 465 Ų buried · 1 hydrogen bond · protein-protein
  • A–C · 464 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

  • 3QLL · Crystal Structure of RipC from Yersinia pestis · the same entry in another collection · chain A against A, TM-score 1.00

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