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Thunberia alata 16:0-acp desaturase

Analyse Thunberia alata 16:0-acp desaturase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7PP7
Type: protein
Length: 311 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acyl-[acyl-carrier-protein] 6-desaturase
EC: 1.14.19.26
UniProt: Q41510
Ligands: FE
Pockets: 3 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 75% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acyl-[acyl-carrier-protein] 6-desaturase (EC 1.14.19.26)	protein	311	75% helix, 3% strand	Q41510

Ligands and binding sites

FE · Fe (III) ion · metal · 2 copies · chains A

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	388	0.71	0.82	38	empty
2	81	0.68	0.93	14	empty
3	90	0.38	0.76	22	empty

Compared structures

7PP7 · Thunberia alata 16:0-ACP desaturase · the same entry in another collection · chain A against A, TM-score 1.00
Q41510 · AlphaFold monomer V2.0 prediction for acyl-[acyl-carrier-protein] 6-desaturase (Q41510) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 Q41510
Elsewhere: RCSB PDB 7PP7 · PDBe 7PP7 · UniProt Q41510

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