MolNFT v1 · #21822 · protein
A single mutation of P450 BM3 induces the conformational rearrangement seen upon substrate-binding in wild-type enzyme
1SMI · Bifunctional P-450:NADPH-P450 reductase: “A single mutation of P450 BM3 induces the conformational rearrangement seen upon substrate-binding in…”. X-ray diffraction, 1 ligand (HEM), 6 pockets (best druggability 0.88). MolNFT v1…
- PDB
- 1SMI
- Type
- protein
- Length
- 894 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional P-450:NADPH-P450 reductase
- EC
- 1.14.14.1
- UniProt
- P14779
- Ligands
- HEM
- Pockets
- 6 · best druggability 0.88
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional P-450:NADPH-P450 reductase (EC 1.14.14.1) | protein | 439 | 52% helix, 12% strand | P14779 |
| B | Bifunctional P-450:NADPH-P450 reductase (EC 1.14.14.1) | protein | 455 | 53% helix, 11% strand | P14779 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 619 | 0.88 | 0.93 | 89 | HEM |
| 2 | 639 | 0.88 | 0.92 | 79 | HEM |
| 3 | 158 | 0.59 | 0.83 | 28 | empty |
| 4 | 226 | 0.57 | 0.79 | 29 | empty |
| 5 | 253 | 0.51 | 0.75 | 31 | empty |
Compared structures
- 1SMI · A single mutation of P450 BM3 induces the conformational rearrangement seen upon… · the same entry in another collection · chain A against A, TM-score 1.00
- P14779 · AlphaFold monomer V2.0 prediction for bifunctional cytochrome P450/NADPH--P450 reductase… · a predicted model of the same protein · chain B 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 P14779
- Elsewhere: RCSB PDB 1SMI · PDBe 1SMI · UniProt P14779
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