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In meso structure of the membrane integral lipoprotein intramolecular transacylase Lit from Bacillus cereus with H85A mutation

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PDB: 7B0Q
Type: protein
Length: 220 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.42
Source: Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB…
Molecule: Hypothetical Membrane Spanning Protein
UniProt: Q813T3
Pockets: 2 · best druggability 0.74

Structure

x-ray diffraction · resolution 2.42 · 1 distinct chain · 77% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical Membrane Spanning Protein	protein	220	77% helix, 0% strand	Q813T3

Ligands and binding sites

OLC · (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate · additive · 7 copies · chains A
GOL · Glycerol · additive · 3 copies · chains A
CIT · Citric acid · additive · 2 copies · chains A
PG5 · 1-methoxy-2-[2-(2-methoxy-ethoxy]-ethane · additive · chains A

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

Pockets

2 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	836	0.74	0.78	52	OLC
2	57	0.28	0.74	18	empty

Compared structures

7B0Q · In meso structure of the membrane integral lipoprotein intramolecular transacylase lit… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q813T3
Elsewhere: RCSB PDB 7B0Q · PDBe 7B0Q · UniProt Q813T3

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