MolNFT v1 · #176927 · protein

Crystal structure of two pericyclases catalyzing [4+2] cycloaddition

7E22 · Diels-alderase FSA2: “Crystal structure of two pericyclases catalyzing [4+2] cycloaddition”. X-ray diffraction, 1 ligand (HVF), 2 pockets (best druggability 0.80). MolNFT v1 #176927 on GenesisL1: 3D structure, binding sites and…

PDB: 7E22
Type: protein
Length: 366 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Diels-alderase FSA2
EC: 5.5.1.-
UniProt: A0A0E4AYE7
Ligands: HVF
Pockets: 2 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Diels-alderase FSA2 (EC 5.5.1.-)	protein	366	2% helix, 54% strand	A0A0E4AYE7

Ligands and binding sites

HVF · Equisetin · ligand · chains A

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

Pockets

2 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	486	0.80	0.87	47	HVF
2	55	0.27	0.73	20	empty

Compared structures

7E22 · Crystal structure of two pericyclases catalyzing [4+2] cycloaddition · 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 A0A0E4AYE7
Elsewhere: RCSB PDB 7E22 · PDBe 7E22 · UniProt A0A0E4AYE7

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