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1.65 ångström crystal structure of the CYS71VAL variant in the fungal photoreceptor vvd

Analyse 1.65 ångström crystal structure of the CYS71VAL variant in the fungal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3D72
Type: protein
Length: 298 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Vivid pas protein vvd
UniProt: Q9C3Y6
Ligands: FAD
Pockets: 4 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Vivid pas protein vvd	protein	149	26% helix, 24% strand	Q9C3Y6

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · 2 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	239	0.72	0.87	30	FAD
2	231	0.72	0.87	33	FAD
3	96	0.34	0.73	20	empty
4	73	0.33	0.75	19	empty

Interfaces

1 interface between chains.

A–B · 637 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

3D72 · 1.65 Angstrom crystal structure of the Cys71Val variant in the fungal photoreceptor VVD · 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 Q9C3Y6
Elsewhere: RCSB PDB 3D72 · PDBe 3D72 · UniProt Q9C3Y6

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