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Crystal structure of low temperature requirement C protein from listeria monocytogenes

Analyse Crystal structure of low temperature requirement C protein from listeria… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1Y9I
Type
protein
Length
636 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Low temperature requirement C protein
UniProt
Q9ZIM5
Ligands
CA, MG
Pockets
7 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 68% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DLow temperature requirement C proteinprotein15968% helix, 0% strandQ9ZIM5

Ligands and binding sites

  • CA · Calcium ion · metal · 4 copies · chains A, B, C, D
  • MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
  • GOL · Glycerol · additive · chains B, C, D

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

Pockets

7 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11240.790.9727empty
22750.600.7928empty
32570.590.8030CA
43180.590.7738empty
52470.580.8027empty

Interfaces

6 interfaces between chains.

  • A–D · 1158 Ų buried · 6 hydrogen bonds · protein-protein
  • B–C · 1126 Ų buried · 6 hydrogen bonds · protein-protein
  • C–D · 1010 Ų buried · 5 hydrogen bonds · protein-protein
  • A–B · 1007 Ų buried · 5 hydrogen bonds · protein-protein
  • A–C · 390 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

  • 1Y9I · Crystal structure of low temperature requirement C protein from Listeria monocytogenes · the same entry in another collection · chain A against A, TM-score 1.00

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