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Crystal structure of a putative 4-hydroxy-2-oxoglutarate aldolase from bacillus cereus

Analyse Crystal structure of a putative 4-hydroxy-2-oxoglutarate aldolase from bacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3N73
Type: protein
Length: 499 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative 4-hydroxy-2-oxoglutarate aldolase
UniProt: Q72YM0
Ligands: CL
Pockets: 1 · best druggability 0.36

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative 4-hydroxy-2-oxoglutarate aldolase	protein	250	43% helix, 18% strand	Q72YM0
B	Putative 4-hydroxy-2-oxoglutarate aldolase	protein	249	43% helix, 18% strand	Q72YM0

Ligands and binding sites

CL · Chloride ion · ion · 3 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	62	0.36	0.78	24	empty

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

3N73 · Crystal structure of a putative 4-hydroxy-2-oxoglutarate aldolase from Bacillus cereus · 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 Q72YM0
Elsewhere: RCSB PDB 3N73 · PDBe 3N73 · UniProt Q72YM0

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