Research workbench

Crystal structure of the loading gnatl domain of cura from lyngbya majuscula

Analyse Crystal structure of the loading gnatl domain of cura from lyngbya majuscula in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2REE
Type: protein
Length: 398 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cura
EC: 2.3.1.38, 4.1.1.9
UniProt: Q6DNF2
Ligands: SO4, CL
Pockets: 2 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cura (EC 2.3.1.38, 4.1.1.9)	protein	199	35% helix, 24% strand	Q6DNF2

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A, B
CL · Chloride ion · ion · chains A
GOL · Glycerol · additive · 2 copies · chains A, B

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	928	0.83	0.85	116	SO4, GOL
2	65	0.38	0.79	16	empty

Interfaces

1 interface between chains.

A–B · 484 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

2REE · Crystal structure of the loading GNATL domain of CurA from Lyngbya majuscula · 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 Q6DNF2
Elsewhere: RCSB PDB 2REE · PDBe 2REE · UniProt Q6DNF2

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.