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Structure of a propionaldehyde dehydrogenase from the clostridium phytofermentans fucose utilisation bacterial microcompartment

Analyse Structure of a propionaldehyde dehydrogenase from the clostridium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4C3S
Type: protein
Length: 435 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aldehyde dehydrogenase
EC: 1.2.1.10
UniProt: A9KN57
Ligands: NAD, SO4
Pockets: 1 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aldehyde dehydrogenase (EC 1.2.1.10)	protein	435	45% helix, 21% strand	A9KN57

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
SO4 · Sulfate ion · ion · 5 copies · 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	270	0.58	0.78	43	NAD

Compared structures

4C3S · Structure of a propionaldehyde dehydrogenase from the Clostridium phytofermentans fucose… · 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 A9KN57
Elsewhere: RCSB PDB 4C3S · PDBe 4C3S · UniProt A9KN57

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