MolNFT v1 · #50349 · protein
Crystal structure of 3-hsa hydroxylase from rhodococcus sp. RHA1
2RFQ · 3-hsa hydroxylase, oxygenase: “Crystal structure of 3-hsa hydroxylase from rhodococcus sp. RHA1”. X-ray diffraction, 1 ligand (1PS), 16 pockets (best druggability 0.71). MolNFT v1 #50349 on GenesisL1: 3D structure, binding sites and…
- PDB
- 2RFQ
- Type
- protein
- Length
- 1,532 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-hsa hydroxylase, oxygenase
- UniProt
- Q0S811
- Ligands
- 1PS
- Pockets
- 16 · best druggability 0.71
Structure
x-ray diffraction · 4 distinct chains · 60% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-hsa hydroxylase, oxygenase | protein | 388 | 59% helix, 16% strand | Q0S811 |
| B | 3-hsa hydroxylase, oxygenase | protein | 387 | 60% helix, 16% strand | Q0S811 |
| C | 3-hsa hydroxylase, oxygenase | protein | 378 | 60% helix, 16% strand | Q0S811 |
| D | 3-hsa hydroxylase, oxygenase | protein | 379 | 60% helix, 16% strand | Q0S811 |
Ligands and binding sites
- 1PS · 3-pyridinium-1-ylpropane-1-sulfonate · ligand · 13 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 380 | 0.71 | 0.83 | 60 | empty |
| 2 | 387 | 0.71 | 0.82 | 59 | empty |
| 3 | 413 | 0.70 | 0.81 | 60 | empty |
| 4 | 335 | 0.70 | 0.82 | 52 | empty |
| 5 | 263 | 0.67 | 0.84 | 49 | empty |
Interfaces
6 interfaces between chains.
- A–D · 1604 Ų buried · 32 hydrogen bonds · protein-protein
- B–C · 1559 Ų buried · 31 hydrogen bonds · protein-protein
- C–D · 1179 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 1169 Ų buried · 22 hydrogen bonds · protein-protein
- A–C · 133 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 32 modified (engineered).
Compared structures
- 2RFQ · Crystal structure of 3-HSA hydroxylase from Rhodococcus sp. RHA1 · the same entry in another collection · chain D against D, TM-score 1.00
- Q0S811 · AlphaFold monomer V2.0 prediction for flavin-dependent monooxygenase, oxygenase subunit… · a predicted model of the same protein · chain C against A, TM-score 0.98
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 Q0S811
- Elsewhere: RCSB PDB 2RFQ · PDBe 2RFQ · UniProt Q0S811
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