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Crystal structure of the vibrio cholerae cytolysin (hlya) heptameric pore

Analyse Crystal structure of the vibrio cholerae cytolysin (hlya) heptameric pore in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3O44
Type: protein
Length: 8,134 residues
Chains: 14
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hemolysin
UniProt: C2C744
Pockets: 20 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N	Hemolysin	protein	581	4% helix, 53% strand	C2C744

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	924	0.79	0.81	128	empty
2	984	0.77	0.80	129	empty
3	1157	0.76	0.79	119	empty
4	637	0.75	0.82	89	empty
5	891	0.75	0.79	95	empty

Interfaces

32 interfaces between chains.

M–N · 2866 Å² buried · 77 hydrogen bonds · protein-protein
A–B · 2857 Å² buried · 72 hydrogen bonds · protein-protein
H–N · 2844 Å² buried · 64 hydrogen bonds · protein-protein
A–G · 2843 Å² buried · 70 hydrogen bonds · protein-protein
J–K · 2840 Å² buried · 64 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 42 disulfide (disulfide).

Compared structures

3O44 · Crystal Structure of the Vibrio cholerae Cytolysin (HlyA) Heptameric Pore · 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 C2C744
Elsewhere: RCSB PDB 3O44 · PDBe 3O44 · UniProt C2C744

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