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Structure of the S. cerevisiae alpha-mannosidase 1

Analyse Structure of the S. cerevisiae alpha-mannosidase 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5JM0
Type: protein
Length: 940 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-MANNOSIDASE,ALPHA-MANNOSIDASE,ALPHA-mannosidase
EC: 3.2.1.24
UniProt: P22855
Pockets: 20 · best druggability 0.85

Structure

electron microscopy · 1 distinct chain · 23% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-MANNOSIDASE,ALPHA-MANNOSIDASE,ALPHA-mannosidase (EC 3.2.1.24)	protein	940	23% helix, 21% strand	P22855

Pockets

20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1166	0.85	0.86	110	empty
2	461	0.81	0.89	67	empty
3	57	0.74	0.99	19	empty
4	873	0.73	0.77	92	empty
5	105	0.71	0.93	28	empty

Compared structures

5JM0 · Structure of the S. cerevisiae alpha-mannosidase 1 · the same entry in another collection · chain A against A, TM-score 1.00
P22855 · AlphaFold monomer V2.0 prediction for alpha-mannosidase (P22855) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 P22855
Elsewhere: RCSB PDB 5JM0 · PDBe 5JM0 · UniProt P22855

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