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13-meric clya pore complex

Analyse 13-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: 6MRU
Type: protein
Length: 3,705 residues
Chains: 13
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hemolysin E, chromosomal
UniProt: P77335
Pockets: 20 · best druggability 0.72

Structure

electron microscopy · 1 distinct chain · 90% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L, M	Hemolysin E, chromosomal	protein	285	90% 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	836	0.72	0.77	107	empty
2	458	0.64	0.77	55	empty
3	350	0.62	0.77	55	empty
4	297	0.59	0.78	51	empty
5	190	0.59	0.81	33	empty

Interfaces

13 interfaces between chains.

A–B · 2436 Å² buried · 26 hydrogen bonds · protein-protein
L–M · 2409 Å² buried · 25 hydrogen bonds · protein-protein
J–K · 2344 Å² buried · 23 hydrogen bonds · protein-protein
H–I · 2343 Å² buried · 24 hydrogen bonds · protein-protein
K–L · 2341 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

6MRU · 13-meric ClyA pore complex · the same entry in another collection · chain M against M, 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 6MRU · PDBe 6MRU · UniProt P77335

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