Research workbench

N249Y mutant of the alcohol dehydrogenase from the archaeon sulfolobus solfataricus-tetragonal crystal form

Analyse N249Y mutant of the alcohol dehydrogenase from the archaeon sulfolobus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1NVG
Type: protein
Length: 347 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NAD-dependent alcohol dehydrogenase
EC: 1.1.1.1
UniProt: P39462
Ligands: ZN
Pockets: 2 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NAD-dependent alcohol dehydrogenase (EC 1.1.1.1)	protein	347	31% helix, 27% strand	P39462

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · 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	475	0.68	0.79	52	empty
2	59	0.31	0.75	16	empty

Compared structures

1NVG · N249Y mutant of the alcohol dehydrogenase from the archaeon sulfolobus… · the same entry in another collection · chain A against A, TM-score 1.00
P39462 · AlphaFold monomer V2.0 prediction for NAD-dependent alcohol dehydrogenase (P39462) · a predicted model of the same protein · 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 P39462
Elsewhere: RCSB PDB 1NVG · PDBe 1NVG · UniProt P39462

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