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The structure of the karrikin insensitive (KAI2) protein in arabidopsis thaliana

Analyse The structure of the karrikin insensitive (KAI2) protein in arabidopsis thaliana in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4HTA
Type: protein
Length: 271 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hydrolase, ALPHA/BETA fold family protein
UniProt: Q9SZU7
Ligands: PO4
Pockets: 2 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hydrolase, ALPHA/BETA fold family protein	protein	271	47% helix, 18% strand	Q9SZU7

Ligands and binding sites

PO4 · Phosphate ion · ion · chains A
GOL · Glycerol · additive · 5 copies · chains A

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	105	0.68	0.91	26	GOL
2	57	0.32	0.76	14	empty

Compared structures

4HTA · The structure of the karrikin insensitive (KAI2) protein in Arabidopsis thaliana · the same entry in another collection · chain A against A, TM-score 1.00
Q9SZU7 · AlphaFold monomer V2.0 prediction for probable esterase KAI2 (Q9SZU7) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q9SZU7
Elsewhere: RCSB PDB 4HTA · PDBe 4HTA · UniProt Q9SZU7

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