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Crystal structure of the lon-like protease mtalonc in complex with lactacystin

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

PDB: 4FWG
Type: protein
Length: 594 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: SLA, PO4
Pockets: 7 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	TTC1975 peptidase (EC 3.4.21.53)	protein	594	42% helix, 20% strand	C9DRU9

Ligands and binding sites

SLA · Omuralide, open form · ligand · chains A
PO4 · Phosphate ion · ion · chains A

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

Pockets

7 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	316	0.62	0.79	21	empty
2	244	0.62	0.81	35	SLA
3	125	0.57	0.84	15	empty
4	88	0.51	0.83	15	empty
5	83	0.49	0.82	21	empty

Modifications

Observed in the structure: 9 modified, 1 covalent (engineered, covalent ligand).

Compared structures

4FWG · Crystal structure of the Lon-like protease MtaLonC in complex with lactacystin · 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 4FWG · PDBe 4FWG · UniProt C9DRU9

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