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Crystal structure of abscisic acid receptor PYL2 at 1.55 a

Analyse Crystal structure of abscisic acid receptor PYL2 at 1.55 a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3KL1
Type: protein
Length: 351 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative uncharacterized protein AT2G26040
UniProt: O80992
Pockets: 3 · best druggability 0.87

Structure

x-ray diffraction · 2 distinct chains · 29% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative uncharacterized protein AT2G26040	protein	176	29% helix, 38% strand	O80992
B	Putative uncharacterized protein AT2G26040	protein	175	29% helix, 35% strand	O80992

Pockets

3 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	877	0.87	0.89	71	empty
2	142	0.39	0.73	36	empty
3	84	0.36	0.76	19	empty

Interfaces

1 interface between chains.

A–B · 936 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

3KL1 · Crystal structure of abscisic acid receptor PYL2 at 1.55 A · 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 3KL1 · PDBe 3KL1 · UniProt O80992

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