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ENDO180 D1-4, trigonal form

Analyse ENDO180 D1-4, trigonal form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5AO6
Type: protein
Length: 866 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: C-type mannose receptor 2
UniProt: Q9UBG0
Pockets: 8 · best druggability 0.54

Structure

x-ray diffraction · 2 distinct chains · 14% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	C-type mannose receptor 2	protein	430	13% helix, 33% strand	Q9UBG0
B	C-type mannose receptor 2	protein	436	15% helix, 34% strand	Q9UBG0

Pockets

8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	258	0.54	0.77	40	empty
2	304	0.52	0.74	33	empty
3	176	0.46	0.75	24	empty
4	151	0.44	0.75	22	empty
5	162	0.42	0.74	20	empty

Interfaces

1 interface between chains.

A–B · 519 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 22 disulfide (disulfide).

Compared structures

5AO6 · Endo180 D1-4, trigonal form · the same entry in another collection · chain A against A, TM-score 1.00
Q9UBG0 · AlphaFold monomer V2.0 prediction for C-type mannose receptor 2 (Q9UBG0) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q9UBG0
Elsewhere: RCSB PDB 5AO6 · PDBe 5AO6 · UniProt Q9UBG0

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