MolNFT v1 · #123687 · protein

Crystal structure of a NAD-dependent aldehyde dehydrogenase from burkholderia multivorans in covalent complex with NAD

5JRY: “Crystal structure of a NAD-dependent aldehyde dehydrogenase from burkholderia multivorans in covalent complex…”. X-ray diffraction, 1 ligand (NDP), 3 pockets (best druggability 0.68). MolNFT v1 #123687 on GenesisL1: 3D structure…

PDB: 5JRY
Type: protein
Length: 477 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NAD-dependent aldehyde dehydrogenase
EC: 1.2.1.-
UniProt: A0A0H3KPC8
Ligands: NDP
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NAD-dependent aldehyde dehydrogenase (EC 1.2.1.-)	protein	477	41% helix, 21% strand	A0A0H3KPC8

Ligands and binding sites

NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
GOL · Glycerol · additive · 2 copies · chains A
ACT · Acetate ion · additive · chains A

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

Pockets

3 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	328	0.68	0.82	46	NDP
2	79	0.35	0.76	17	empty
3	55	0.29	0.75	11	empty

Modifications

Observed in the structure: 1 covalent (covalent ligand).

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 A0A0H3KPC8
Elsewhere: RCSB PDB 5JRY · PDBe 5JRY · UniProt A0A0H3KPC8

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