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Crystal structure of the proaerolysin mutant Y221G

Analyse Crystal structure of the proaerolysin mutant Y221G in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3C0M
Type: protein
Length: 898 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aerolysin
UniProt: P09167
Pockets: 9 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 18% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Aerolysin	protein	449	18% helix, 41% strand	P09167

Pockets

9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1159	0.78	0.80	109	empty
2	963	0.78	0.80	84	empty
3	519	0.65	0.77	50	empty
4	299	0.60	0.78	32	empty
5	250	0.59	0.79	40	empty

Interfaces

1 interface between chains.

A–B · 2456 Å² buried · 22 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

3C0M · Crystal structure of the proaerolysin mutant Y221G · 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 B against A, TM-score 0.97

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 3C0M · PDBe 3C0M · UniProt P09167

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