MolNFT v1 · #127111 · protein

Aba receptor from citrus, CSPYL1

5MMX · CSPYL1_ABA: “Aba receptor from citrus, CSPYL1”. X-ray diffraction, 1 ligand (A8S), 4 pockets (best druggability 0.83). MolNFT v1 #127111 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5MMX
Type: protein
Length: 372 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CSPYL1_ABA
UniProt: A0A067E666
Ligands: A8S
Pockets: 4 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A	CSPYL1_ABA	protein	186	27% helix, 36% strand	A0A067E666

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 · 2 copies · chains B, A

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

Pockets

4 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	851	0.83	0.85	64	A8S
2	87	0.33	0.73	21	empty
3	64	0.29	0.74	18	empty
4	61	0.27	0.73	12	empty

Interfaces

1 interface between chains.

B–A · 920 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

5MMX · Aba receptor from citrus, CSPYL1 · 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 A0A067E666
Elsewhere: RCSB PDB 5MMX · PDBe 5MMX · UniProt A0A067E666

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