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Human mitoneet with 2FE-2S coordinating ligand his 87 replaced with cys

Analyse Human mitoneet with 2FE-2S coordinating ligand his 87 replaced with cys in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3LPQ
Type
protein
Length
149 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cdgsh iron sulfur domain-containing protein 1
UniProt
Q9NZ45
Ligands
FES
Pockets
1 · best druggability 0.29

Structure

x-ray diffraction · 2 distinct chains · 16% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACdgsh iron sulfur domain-containing protein 1protein7516% helix, 21% strandQ9NZ45
BCdgsh iron sulfur domain-containing protein 1protein7416% helix, 20% strandQ9NZ45

Ligands and binding sites

  • FES · Fe2/s2 (inorganic) cluster · ligand · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1540.290.7517empty

Interfaces

1 interface between chains.

  • A–B · 2156 Ų buried · 47 hydrogen bonds · protein-protein

Compared structures

  • 3LPQ · Human MitoNEET with 2Fe-2S Coordinating Ligand His 87 Replaced With Cys · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9NZ45 · AlphaFold monomer V2.0 prediction for cdgsh iron-sulfur domain- containing protein 1… · a predicted model of the same protein · chain B against A, TM-score 0.93

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