Research workbench
Plantago major multifunctional oxidoreductase in complex with progesterone and NADP+
Analyse Plantago major multifunctional oxidoreductase in complex with progesterone and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GSD
- Type
- protein
- Length
- 364 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Progesterone 5-beta-reductase
- EC
- 1.1.1.145
- UniProt
- D6N9X1
- Ligands
- STR, NAD
- Pockets
- 1 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Progesterone 5-beta-reductase (EC 1.1.1.145) | protein | 364 | 41% helix, 13% strand | D6N9X1 |
Ligands and binding sites
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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 510 | 0.84 | 0.90 | 67 | STR, NAD |
Compared structures
- 6GSD · Plantago Major multifunctional oxidoreductase in complex with progesterone and NADP+ · 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 D6N9X1
- Elsewhere: RCSB PDB 6GSD · PDBe 6GSD · UniProt D6N9X1
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