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Crystal Structure of Rhodobacter Sphaeroides LOV protein

Analyse Crystal Structure of Rhodobacter Sphaeroides LOV protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4HIA
Type: protein
Length: 352 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.952
Source: Rhodobacter sphaeroides
Molecule: LOV protein
Ligands: FMN, SO4
Pockets: 4 · best druggability 0.75

Structure

x-ray diffraction · resolution 1.952 · 1 distinct chain · 49% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	LOV protein	protein	176	49% helix, 22% strand	—

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
SO4 · Sulfate ion · ion · 4 copies · chains A, B

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

Pockets

4 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	186	0.75	0.91	24	FMN
2	179	0.74	0.90	23	FMN
3	280	0.66	0.83	55	SO4
4	152	0.58	0.83	27	empty

Interfaces

1 interface between chains.

A–B · 885 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

4HIA · Crystal structure of rhodobacter sphaeroides lov protein · 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
Elsewhere: RCSB PDB 4HIA · PDBe 4HIA

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