Research workbench

Crystal structure of a novel engineered diels-alderase: DA_20_00_A74I

Analyse Crystal structure of a novel engineered diels-alderase: DA_20_00_A74I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3I1C
Type: protein
Length: 314 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Diisopropyl-fluorophosphatase
EC: 3.1.8.2
UniProt: Q7SIG4
Pockets: 2 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 1% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Diisopropyl-fluorophosphatase (EC 3.1.8.2)	protein	314	1% helix, 51% strand	Q7SIG4

Ligands and binding sites

GOL · Glycerol · additive · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	61	0.71	0.97	19	empty
2	198	0.61	0.82	31	empty

Compared structures

3I1C · Crystal Structure of a Novel Engineered Diels-Alderase: DA_20_00_A74I · the same entry in another collection · chain A against A, TM-score 1.00
Q7SIG4 · AlphaFold monomer V2.0 prediction for diisopropyl-fluorophosphatase (Q7SIG4) · a predicted model of the same protein · chain A 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 Q7SIG4
Elsewhere: RCSB PDB 3I1C · PDBe 3I1C · UniProt Q7SIG4

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