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Structure of S. cerevesiae MAPE1 dodecamer

Analyse Structure of S. cerevesiae MAPE1 dodecamer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5JM9
Type
protein
Length
438 residues
Chains
1
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Vacuolar aminopeptidase 1
EC
3.4.11.22
UniProt
P14904
Pockets
5 · best druggability 0.45

Structure

electron microscopy · 1 distinct chain · 32% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AVacuolar aminopeptidase 1 (EC 3.4.11.22)protein43832% helix, 26% strandP14904

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1950.450.7920empty
21310.440.7726empty
3570.430.8318empty
41180.380.7421empty
5570.320.769empty

Compared structures

  • 5JM9 · Structure of S. cerevesiae mApe1 dodecamer · the same entry in another collection · chain A against A, TM-score 1.00
  • P14904 · AlphaFold monomer V2.0 prediction for vacuolar aminopeptidase 1 (P14904) · a predicted model of the same protein · chain A against A, TM-score 0.99

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