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14-meric clya pore complex

Analyse 14-meric clya pore complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6MRW
Type: protein
Length: 3,990 residues
Chains: 14
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hemolysin E, chromosomal
UniProt: P77335
Pockets: 20 · best druggability 0.73

Structure

electron microscopy · 1 distinct chain · 89% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N	Hemolysin E, chromosomal	protein	285	89% helix, 0% strand	P77335

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	993	0.73	0.76	115	empty
2	818	0.70	0.75	100	empty
3	373	0.65	0.79	58	empty
4	422	0.63	0.77	48	empty
5	420	0.62	0.76	52	empty

Interfaces

14 interfaces between chains.

B–C · 2245 Å² buried · 9 hydrogen bonds · protein-protein
M–N · 2235 Å² buried · 9 hydrogen bonds · protein-protein
D–E · 2179 Å² buried · 7 hydrogen bonds · protein-protein
E–F · 2157 Å² buried · 7 hydrogen bonds · protein-protein
G–H · 2156 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

6MRW · 14-meric ClyA pore complex · the same entry in another collection · chain N against N, 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 P77335
Elsewhere: RCSB PDB 6MRW · PDBe 6MRW · UniProt P77335

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