Research workbench

Crystal structure of the H277A mutant of ADH/D1, an archaeal halo- thermophilic red sea brine pool alcohol dehydrogenase

Analyse Crystal structure of the H277A mutant of ADH/D1, an archaeal halo- thermophilic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5YVR
Type: protein
Length: 403 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alcohol dehydrogenase
UniProt: A0A133UP32
Ligands: NDP, MN
Pockets: 2 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alcohol dehydrogenase	protein	403	55% helix, 10% strand	A0A133UP32

Ligands and binding sites

NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
MN · Manganese (II) ion · metal · chains A

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

Pockets

2 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	678	0.76	0.81	76	NDP
2	66	0.32	0.76	15	empty

Compared structures

5YVR · Crystal Structure of the H277A mutant of ADH/D1, an archaeal halo-thermophilic Red Sea… · 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 A0A133UP32
Elsewhere: RCSB PDB 5YVR · PDBe 5YVR · UniProt A0A133UP32

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.