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The crystal structure of 3-alpha-hydroxysteroid dehydrogenase from comamonas testosteroni, a member of the short chain DEHYDROGENASE/REDUCTASE family

Analyse The crystal structure of 3-alpha-hydroxysteroid dehydrogenase from comamonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1FJH
Type: protein
Length: 472 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3ALPHA-hydroxysteroid DEHYDROGENASE/CARBONYL reductase
EC: 1.1.1.50
UniProt: Q9ZFY9
Pockets: 6 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	3ALPHA-hydroxysteroid DEHYDROGENASE/CARBONYL reductase (EC 1.1.1.50)	protein	236	48% helix, 14% strand	Q9ZFY9

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	51	0.68	0.97	21	empty
2	258	0.53	0.76	48	empty
3	226	0.52	0.76	38	empty
4	51	0.49	0.87	14	empty
5	86	0.37	0.76	21	empty

Interfaces

1 interface between chains.

A–B · 1992 Å² buried · 29 hydrogen bonds · protein-protein

Compared structures

1FJH · The crystal structure of 3-alpha-hydroxysteroid dehydrogenase from comamonas… · 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 Q9ZFY9
Elsewhere: RCSB PDB 1FJH · PDBe 1FJH · UniProt Q9ZFY9

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