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Golgi alpha-mannosidase II

Analyse Golgi alpha-mannosidase II in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6RPC
Type: protein
Length: 1,010 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-mannosidase 2
EC: 3.2.1.114
UniProt: Q24451
Ligands: ZN
Pockets: 11 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-mannosidase 2 (EC 3.2.1.114)	protein	1010	25% helix, 29% strand	Q24451

Ligands and binding sites

ZN · Zinc ion · metal · chains A
EDO · 1,2-ethanediol · additive · 7 copies · chains A
SIN · Succinic acid · additive · chains A

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

Pockets

11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	906	0.82	0.84	122	EDO, SIN
2	151	0.81	0.97	29	empty
3	277	0.64	0.81	32	empty
4	159	0.50	0.78	25	EDO
5	161	0.49	0.78	26	empty

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

6RPC · Golgi alpha-mannosidase II · the same entry in another collection · chain A against A, TM-score 1.00

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 Q24451
Elsewhere: RCSB PDB 6RPC · PDBe 6RPC · UniProt Q24451

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