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Crystal structure of probable PROTEASE/AMIDASE from clostridium acetobutylicum atcc 824

Analyse Crystal structure of probable PROTEASE/AMIDASE from clostridium acetobutylicum… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3MGK
Type: protein
Length: 400 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Intracellular PROTEASE/AMIDASE related enzyme (thij family)
UniProt: Q97FB4
Pockets: 3 · best druggability 0.47

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Intracellular PROTEASE/AMIDASE related enzyme (thij family)	protein	199	36% helix, 22% strand	Q97FB4
B	Intracellular PROTEASE/AMIDASE related enzyme (thij family)	protein	201	34% helix, 21% strand	Q97FB4

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	61	0.47	0.84	18	empty
2	88	0.45	0.81	22	empty
3	56	0.33	0.78	22	empty

Interfaces

1 interface between chains.

A–B · 1627 Å² buried · 26 hydrogen bonds · protein-protein

Compared structures

3MGK · CRYSTAL STRUCTURE OF PROBABLE PROTEASE/AMIDASE FROM Clostridium acetobutylicum ATCC 824 · 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 Q97FB4
Elsewhere: RCSB PDB 3MGK · PDBe 3MGK · UniProt Q97FB4

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