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Crystal structure of the lon-like protease mtalonc

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

PDB: 4FW9
Type: protein
Length: 603 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: TTC1975 peptidase
EC: 3.4.21.53
UniProt: C9DRU9
Ligands: PO4
Pockets: 6 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	TTC1975 peptidase (EC 3.4.21.53)	protein	603	41% helix, 19% strand	C9DRU9

Ligands and binding sites

PO4 · Phosphate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	317	0.65	0.81	26	empty
2	212	0.57	0.79	31	empty
3	107	0.56	0.84	22	empty
4	132	0.53	0.81	15	empty
5	151	0.48	0.77	24	empty

Modifications

Observed in the structure: 7 modified (engineered).

Compared structures

4FW9 · Crystal structure of the Lon-like protease MtaLonC · 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 C9DRU9
Elsewhere: RCSB PDB 4FW9 · PDBe 4FW9 · UniProt C9DRU9

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