MolNFT v1 · #112175 · protein

Structure of yeast D3,D2-enoyl-CoA isomerase bound to sulphate ion

4ZDD · 3,2-trans-enoyl-CoA isomerase: “Structure of yeast D3,D2-enoyl-CoA isomerase bound to sulphate ion”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.59). MolNFT v1 #112175 on GenesisL1: 3D structure, binding sites…

PDB: 4ZDD
Type: protein
Length: 247 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3,2-trans-enoyl-CoA isomerase
EC: 5.3.3.8
UniProt: Q05871
Ligands: SO4
Pockets: 3 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3,2-trans-enoyl-CoA isomerase (EC 5.3.3.8)	protein	247	50% helix, 17% strand	Q05871

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 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	253	0.59	0.79	34	empty
2	53	0.53	0.88	16	SO4
3	58	0.28	0.74	14	empty

Compared structures

4ZDD · Structure of yeast D3,D2-enoyl-CoA isomerase bound to sulphate ion · the same entry in another collection · chain A against A, TM-score 1.00
Q05871 · AlphaFold monomer V2.0 prediction for 3,2-trans-enoyl-CoA isomerase (Q05871) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q05871
Elsewhere: RCSB PDB 4ZDD · PDBe 4ZDD · UniProt Q05871

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