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Crystal structure of 17BETA-HSD1 with dht in normal and reverse orientation.

Analyse Crystal structure of 17BETA-HSD1 with dht in normal and reverse orientation. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3DEY
Type: protein
Length: 277 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Estradiol 17-beta-dehydrogenase 1
EC: 1.1.1.62
UniProt: P14061
Ligands: DHT
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	Estradiol 17-beta-dehydrogenase 1 (EC 1.1.1.62)	protein	277	54% helix, 15% strand	P14061

Ligands and binding sites

DHT · 5-alpha-dihydrotestosterone · ligand · chains X
GOL · Glycerol · additive · chains X

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	646	0.72	0.79	59	DHT

Compared structures

3DEY · Crystal structure of 17beta-HSD1 with DHT in normal and reverse orientation. · the same entry in another collection · chain X against X, TM-score 1.00
P14061 · AlphaFold monomer V2.0 prediction for 17-beta-hydroxysteroid dehydrogenase type 1 (P14061) · a predicted model of the same protein · chain X 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 P14061
Elsewhere: RCSB PDB 3DEY · PDBe 3DEY · UniProt P14061

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