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Crystal structure of N-terminal domain of E.COLI lon protease

Analyse Crystal structure of N-terminal domain of E.COLI lon protease in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ANE
Type: protein
Length: 875 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ATP-dependent protease la
EC: 3.4.21.53
UniProt: P0A9M0
Pockets: 9 · best druggability 0.83

Structure

x-ray diffraction · 3 distinct chains · 12% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D, E, F, G	ATP-dependent protease la (EC 3.4.21.53)	protein	110	13% helix, 54% strand	P0A9M0
B, C	ATP-dependent protease la (EC 3.4.21.53)	protein	108	11% helix, 53% strand	P0A9M0
H	ATP-dependent protease la (EC 3.4.21.53)	protein	109	13% helix, 52% strand	P0A9M0

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	890	0.83	0.84	117	empty
2	622	0.82	0.86	82	empty
3	82	0.66	0.92	29	empty
4	165	0.65	0.86	33	empty
5	53	0.59	0.91	24	empty

Interfaces

14 interfaces between chains.

A–B · 1044 Å² buried · 25 hydrogen bonds · protein-protein
C–D · 979 Å² buried · 33 hydrogen bonds · protein-protein
E–F · 951 Å² buried · 18 hydrogen bonds · protein-protein
G–H · 937 Å² buried · 23 hydrogen bonds · protein-protein
D–G · 320 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

2ANE · Crystal structure of N-terminal domain of E.Coli Lon Protease · the same entry in another collection · chain H against H, TM-score 1.00
P0A9M0 · AlphaFold monomer V2.0 prediction for lon protease (P0A9M0) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P0A9M0
Elsewhere: RCSB PDB 2ANE · PDBe 2ANE · UniProt P0A9M0

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