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Crystal structure of the R103K mutant of aspartate semialdehyde dehydrogenase from haemophilus influenzae

Analyse Crystal structure of the R103K mutant of aspartate semialdehyde dehydrogenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PR3
Type: protein
Length: 357 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aspartate semialdehyde dehydrogenase
EC: 1.2.1.11
UniProt: P44801
Ligands: PO4
Pockets: 1 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aspartate semialdehyde dehydrogenase (EC 1.2.1.11)	protein	357	42% helix, 23% strand	P44801

Ligands and binding sites

PO4 · Phosphate ion · ion · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	280	0.56	0.77	36	empty

Compared structures

1PR3 · Crystal Structure of the R103K Mutant of Aspartate Semialdehyde dehydrogenase from… · the same entry in another collection · chain A against A, TM-score 1.00
P44801 · AlphaFold monomer V2.0 prediction for aspartate-semialdehyde dehydrogenase (P44801) · 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 P44801
Elsewhere: RCSB PDB 1PR3 · PDBe 1PR3 · UniProt P44801

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