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Crystal structure of a DUF4931 family protein (BCE0241) from bacillus cereus atcc 10987 at 2.65 a resolution

Analyse Crystal structure of a DUF4931 family protein (BCE0241) from bacillus cereus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4QVU
Type: protein
Length: 217 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
UniProt: Q73EW7
Ligands: ZN, NA
Pockets: 3 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein	protein	217	28% helix, 31% strand	Q73EW7

Ligands and binding sites

ZN · Zinc ion · metal · chains A
NA · Sodium ion · metal · chains A
PG4 · Tetraethylene glycol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	176	0.56	0.80	27	empty
2	154	0.47	0.76	25	empty
3	56	0.37	0.80	17	PG4

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

4QVU · Crystal structure of a DUF4931 family protein (BCE0241) from Bacillus cereus ATCC 10987… · 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 Q73EW7
Elsewhere: RCSB PDB 4QVU · PDBe 4QVU · UniProt Q73EW7

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