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Structure of chloroflexus islandicus lov domain C85A variant (cisfbfp)

Analyse Structure of chloroflexus islandicus lov domain C85A variant (cisfbfp) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7OO9
Type: protein
Length: 212 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hybrid sensor histidine KINASE/RESPONSE regulator
UniProt: A0A178LR65
Ligands: FMN
Pockets: 3 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Hybrid sensor histidine KINASE/RESPONSE regulator	protein	106	25% helix, 38% strand	A0A178LR65

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
GOL · Glycerol · additive · 10 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	184	0.72	0.89	22	FMN
2	192	0.72	0.88	24	FMN
3	163	0.49	0.77	21	empty

Interfaces

1 interface between chains.

A–B · 668 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

7OO9 · Structure of Chloroflexus islandicus LOV domain C85A variant (CisFbFP) · 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 A0A178LR65
Elsewhere: RCSB PDB 7OO9 · PDBe 7OO9 · UniProt A0A178LR65

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