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Crystal structure of abscisic acid-bound PYL2

Analyse Crystal structure of abscisic acid-bound PYL2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3KB0
Type: protein
Length: 176 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative uncharacterized protein AT2G26040
UniProt: O80992
Ligands: A8S
Pockets: 1 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative uncharacterized protein AT2G26040	protein	176	28% helix, 38% strand	O80992

Ligands and binding sites

A8S · (2Z,4E)-5-[(1S)-1-hydroxy-2,6,6-trimethyl-4-oxocyclohex-2-en-1-yl]-3-methylpenta-2,4-dienoic acid · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	269	0.85	0.96	31	A8S

Compared structures

3KB0 · Crystal structure of abscisic acid-bound PYL2 · the same entry in another collection · chain A against A, TM-score 1.00
O80992 · AlphaFold monomer V2.0 prediction for abscisic acid receptor PYL2 (O80992) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 O80992
Elsewhere: RCSB PDB 3KB0 · PDBe 3KB0 · UniProt O80992

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