Research workbench

Aba receptor from citrus, CSPYL1

Analyse Aba receptor from citrus, CSPYL1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5MN0
Type: protein
Length: 482 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CSPYL1; Protein phosphatase 2C 16
EC: 3.1.3.16
UniProt: A0A067E666, Q9CAJ0
Ligands: A8S, MN, CL
Pockets: 5 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CSPYL1	protein	187	28% helix, 36% strand	A0A067E666
B	Protein phosphatase 2C 16 (EC 3.1.3.16)	protein	295	31% helix, 30% strand	Q9CAJ0

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
MN · Manganese (II) ion · metal · 3 copies · chains B
CL · Chloride ion · ion · 6 copies · chains B
GOL · Glycerol · additive · chains B

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

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	229	0.84	0.97	30	A8S
2	55	0.71	0.98	19	empty
3	244	0.56	0.78	29	MN, CL
4	74	0.42	0.80	19	empty
5	73	0.31	0.74	19	CL

Interfaces

1 interface between chains.

A–B · 847 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

5MN0 · Aba receptor from citrus, CSPYL1 · the same entry in another collection · chain A against A, TM-score 1.00
Q9CAJ0 · AlphaFold monomer V2.0 prediction for protein phosphatase 2C 16 (Q9CAJ0) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 A0A067E666
Every structure of UniProt Q9CAJ0
Elsewhere: RCSB PDB 5MN0 · PDBe 5MN0 · UniProt A0A067E666 · UniProt Q9CAJ0

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