Research workbench
Crystal structure of human 20ALPHA-hsd in ternary complex with NADP and 20ALPHA-hydroxy-progesterone
Analyse Crystal structure of human 20ALPHA-hsd in ternary complex with NADP and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MRQ
- Type
- protein
- Length
- 323 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aldo-keto reductase family 1 member C1
- EC
- 1.1.1.149
- UniProt
- Q04828
- Ligands
- NAP, STR
- Pockets
- 3 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aldo-keto reductase family 1 member C1 (EC 1.1.1.149) | protein | 323 | 39% helix, 16% strand | Q04828 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- STR · Progesterone · ligand · chains A
- BME · Beta-mercaptoethanol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 497 | 0.76 | 0.84 | 60 | NAP, STR |
| 2 | 69 | 0.44 | 0.81 | 21 | empty |
| 3 | 53 | 0.31 | 0.76 | 17 | BME |
Compared structures
- 1MRQ · Crystal structure of human 20alpha-HSD in ternary complex with NADP and… · the same entry in another collection · chain A against A, TM-score 1.00
- Q04828 · AlphaFold monomer V2.0 prediction for aldo-keto reductase family 1 member C1 (Q04828) · 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 Q04828
- Elsewhere: RCSB PDB 1MRQ · PDBe 1MRQ · UniProt Q04828
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