MolNFT v1 · #157338 · protein

Structure of a bacterial ALDH16 complexed with NAD

6MVS · Aldehyde dehydrogenase: “Structure of a bacterial ALDH16 complexed with NAD”. X-ray diffraction, 2 ligands (NAD, SO4), 5 pockets (best druggability 0.78). MolNFT v1 #157338 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 6MVS
Type: protein
Length: 751 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aldehyde dehydrogenase
UniProt: A0A0Q3EUQ3
Ligands: NAD, SO4
Pockets: 5 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aldehyde dehydrogenase	protein	751	42% helix, 19% strand	A0A0Q3EUQ3

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
SO4 · Sulfate ion · ion · chains A
GOL · Glycerol · additive · chains A

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

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	904	0.78	0.81	67	SO4
2	311	0.68	0.83	53	NAD
3	421	0.63	0.77	53	empty
4	251	0.54	0.76	30	empty
5	64	0.28	0.73	17	empty

Compared structures

6MVS · Structure of a bacterial ALDH16 complexed with NAD · 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 A0A0Q3EUQ3
Elsewhere: RCSB PDB 6MVS · PDBe 6MVS · UniProt A0A0Q3EUQ3

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