Research workbench

Yeast 5-aminolaevulinic acid dehydratase lead (pb) complex

Analyse Yeast 5-aminolaevulinic acid dehydratase lead (pb) complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1QNV
Type: protein
Length: 328 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 5-aminolaevulinic acid dehydratase
EC: 4.2.1.24
UniProt: P05373
Ligands: PB
Pockets: 2 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	5-aminolaevulinic acid dehydratase (EC 4.2.1.24)	protein	328	39% helix, 18% strand	P05373

Ligands and binding sites

PB · Lead (II) ion · metal · 2 copies · 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	306	0.56	0.76	39	PB
2	59	0.36	0.78	13	empty

Compared structures

1QNV · yeast 5-aminolaevulinic acid dehydratase Lead (Pb) complex · the same entry in another collection · chain A against A, TM-score 1.00
P05373 · AlphaFold monomer V2.0 prediction for delta-aminolevulinic acid dehydratase (P05373) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P05373
Elsewhere: RCSB PDB 1QNV · PDBe 1QNV · UniProt P05373

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