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Crystal structure of zucchini (K171A)

Analyse Crystal structure of zucchini (K171A) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4GEM
Type
protein
Length
383 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Mitochondrial cardiolipin hydrolase
EC
3.1.4.-
UniProt
Q9VKD7
Ligands
ZN
Pockets
2 · best druggability 0.30

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMitochondrial cardiolipin hydrolase (EC 3.1.4.-)protein19436% helix, 20% strandQ9VKD7
BMitochondrial cardiolipin hydrolase (EC 3.1.4.-)protein18934% helix, 21% strandQ9VKD7

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A, B
  • EDO · 1,2-ethanediol · additive · 2 copies · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1600.300.7515empty
2730.300.7315empty

Interfaces

1 interface between chains.

  • A–B · 1608 Ų buried · 35 hydrogen bonds · protein-protein

Compared structures

  • 4GEM · Crystal structure of Zucchini (K171A) · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9VKD7 · AlphaFold monomer V2.0 prediction for mitochondrial cardiolipin hydrolase (Q9VKD7) · a predicted model of the same protein · chain B against A, TM-score 0.95

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