Research workbench

17BETA-hydroxysteroid dehydrogenase 14 variant S205 - mutant H93A

Analyse 17BETA-hydroxysteroid dehydrogenase 14 variant S205 - mutant H93A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6HNO
Type: protein
Length: 257 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 17-beta-hydroxysteroid dehydrogenase 14
EC: 1.1.1.-
UniProt: Q9BPX1
Ligands: NAD
Pockets: 1 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	17-beta-hydroxysteroid dehydrogenase 14 (EC 1.1.1.-)	protein	257	50% helix, 15% strand	Q9BPX1

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · ligand · 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	706	0.75	0.81	65	NAD

Compared structures

6HNO · 17beta-hydroxysteroid dehydrogenase 14 variant S205 - mutant H93A · the same entry in another collection · chain A against A, TM-score 1.00
Q9BPX1 · AlphaFold monomer V2.0 prediction for 17-beta-hydroxysteroid dehydrogenase 14 (Q9BPX1) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q9BPX1
Elsewhere: RCSB PDB 6HNO · PDBe 6HNO · UniProt Q9BPX1

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