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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 v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 24.0
Source: Saccharomyces cerevisiae
Molecule: Vacuolar aminopeptidase 1
EC: 3.4.11.22
UniProt: P14904
Pockets: 5 · best druggability 0.45

Structure

electron microscopy · resolution 24.0 · 1 distinct chain · 32% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Vacuolar aminopeptidase 1 (EC 3.4.11.22)	protein	438	32% helix, 26% strand	P14904

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	95	0.45	0.79	20	empty
2	131	0.44	0.77	26	empty
3	57	0.43	0.83	18	empty
4	118	0.38	0.74	21	empty
5	57	0.32	0.76	9	empty

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

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P14904
Elsewhere: RCSB PDB 5JM9 · PDBe 5JM9 · UniProt P14904

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