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Crystal structure of the activated aerolysin mutant H132N

Analyse Crystal structure of the activated aerolysin mutant H132N in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3G4O
Type: protein
Length: 890 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aerolysin
UniProt: P09167
Pockets: 8 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 18% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aerolysin	protein	439	19% helix, 37% strand	P09167
B	Aerolysin	protein	451	18% helix, 40% strand	P09167

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	961	0.79	0.81	88	empty
2	1061	0.79	0.80	88	empty
3	712	0.68	0.76	65	empty
4	444	0.63	0.77	44	empty
5	257	0.58	0.78	43	empty

Interfaces

1 interface between chains.

A–B · 2693 Å² buried · 29 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

3G4O · Crystal structure of the activated aerolysin mutant H132N · the same entry in another collection · chain A against A, TM-score 1.00
P09167 · AlphaFold monomer V2.0 prediction for aerolysin (P09167) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P09167
Elsewhere: RCSB PDB 3G4O · PDBe 3G4O · UniProt P09167

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