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Cryo-EM structure of medicago truncatula HISN5 protein

Analyse Cryo-EM structure of medicago truncatula HISN5 protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7OJ5
Type
protein
Length
4,416 residues
Chains
24
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Imidazoleglycerol-phosphate dehydratase
EC
4.2.1.19
UniProt
I3SDM5
Ligands
MN
Pockets
20 · best druggability 0.78

Structure

electron microscopy · 1 distinct chain · 36% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, V, W, X, YImidazoleglycerol-phosphate dehydratase (EC 4.2.1.19)protein18436% helix, 34% strandI3SDM5

Ligands and binding sites

  • MN · Manganese (II) ion · metal · 48 copies · chains A, J, W, B, I, N, C, F, Q, D, S, H, E, L, Y, T, G, X, M, O, V, R, K, P

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18340.780.8177empty
28660.780.8182empty
310010.780.8080empty
410430.770.8082empty
510450.770.8086empty

Interfaces

60 interfaces between chains.

  • H–Q · 767 Ų buried · 6 hydrogen bonds · protein-protein
  • J–S · 766 Ų buried · 6 hydrogen bonds · protein-protein
  • F–M · 765 Ų buried · 6 hydrogen bonds · protein-protein
  • K–W · 765 Ų buried · 6 hydrogen bonds · protein-protein
  • B–W · 765 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 7OJ5 · Cryo-EM structure of Medicago truncatula HISN5 protein · the same entry in another collection · chain A against A, TM-score 1.00

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