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Crystal structure of 5-aminolevulinic acid dehydratase (alad) from mus musculus

Analyse Crystal structure of 5-aminolevulinic acid dehydratase (alad) from mus musculus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2Z0I
Type: protein
Length: 559 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Delta-aminolevulinic acid dehydratase
EC: 4.2.1.24
UniProt: Q9DD05
Pockets: 5 · best druggability 0.47

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Delta-aminolevulinic acid dehydratase (EC 4.2.1.24)	protein	283	46% helix, 16% strand	Q9DD05
B	Delta-aminolevulinic acid dehydratase (EC 4.2.1.24)	protein	276	46% helix, 17% strand	Q9DD05

Pockets

5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	185	0.47	0.75	26	empty
2	140	0.40	0.74	28	empty
3	57	0.36	0.77	17	empty
4	102	0.34	0.73	20	empty
5	87	0.31	0.72	17	empty

Interfaces

1 interface between chains.

A–B · 2251 Å² buried · 21 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 modified (engineered).

Compared structures

2Z0I · Crystal Structure of 5-aminolevulinic acid dehydratase (ALAD) from Mus musculus · 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 Q9DD05
Elsewhere: RCSB PDB 2Z0I · PDBe 2Z0I · UniProt Q9DD05

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