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Crystal structure of 17BETA-hydroxysteroid dehydrogenase (apo form) from fungus cochliobolus lunatus

Analyse Crystal structure of 17BETA-hydroxysteroid dehydrogenase (apo form) from fungus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3IS3
Type: protein
Length: 260 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 17BETA-hydroxysteroid dehydrogenase
EC: 1.1.1.62
UniProt: O93874
Ligands: CL
Pockets: 2 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	17BETA-hydroxysteroid dehydrogenase (EC 1.1.1.62)	protein	260	49% helix, 14% strand	O93874

Ligands and binding sites

CL · Chloride ion · ion · 2 copies · chains A
PEG · Di(hydroxyethyl)ether · additive · chains A
GOL · Glycerol · additive · 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	631	0.81	0.86	67	CL, PEG, GOL
2	60	0.33	0.77	15	empty

Compared structures

3IS3 · Crystal structure of 17beta-Hydroxysteroid dehydrogenase (Apo form) from fungus… · 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 O93874
Elsewhere: RCSB PDB 3IS3 · PDBe 3IS3 · UniProt O93874

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