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Cystal structure of aspartate semialdehyde dehydrogenase from aspergillus fumigatus

Analyse Cystal structure of aspartate semialdehyde dehydrogenase from aspergillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5JW6
Type: protein
Length: 716 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aspartate-semialdehyde dehydrogenase
EC: 1.2.1.11
UniProt: Q4WWR8
Ligands: SO4
Pockets: 10 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Aspartate-semialdehyde dehydrogenase (EC 1.2.1.11)	protein	358	31% helix, 22% strand	Q4WWR8

Ligands and binding sites

SO4 · Sulfate ion · ion · 5 copies · chains A, B

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

Pockets

10 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	390	0.63	0.78	55	SO4
2	407	0.63	0.78	58	SO4
3	81	0.36	0.76	17	empty
4	74	0.36	0.76	17	SO4
5	107	0.35	0.73	22	empty

Interfaces

1 interface between chains.

A–B · 1766 Å² buried · 43 hydrogen bonds · protein-protein

Compared structures

5JW6 · Cystal structure of aspartate semialdehyde dehydrogenase from Aspergillus fumigatus · 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 Q4WWR8
Elsewhere: RCSB PDB 5JW6 · PDBe 5JW6 · UniProt Q4WWR8

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