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Structure of a blue-shifted luciferase from amydetes vivianii

Analyse Structure of a blue-shifted luciferase from amydetes vivianii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6AAA
Type: protein
Length: 1,076 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Blue-shifted luciferase
EC: 1.13.12.7
Pockets: 17 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Blue-shifted luciferase (EC 1.13.12.7)	protein	540	30% helix, 23% strand	—
B	Blue-shifted luciferase (EC 1.13.12.7)	protein	536	31% helix, 25% strand	—

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

17 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	106	0.79	0.99	24	GOL
2	95	0.78	0.99	21	GOL
3	624	0.71	0.79	68	empty
4	456	0.60	0.75	55	empty
5	158	0.59	0.83	30	empty

Interfaces

1 interface between chains.

A–B · 323 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

6AAA · Structure of a blue-shifted Luciferase from Amydetes vivianii · 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 6AAA · PDBe 6AAA

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