Research workbench
Crystal structure of P450BM3 with N-enanthoyl-L-prolyl-L-phenylalanine
Analyse Crystal structure of P450BM3 with N-enanthoyl-L-prolyl-L-phenylalanine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6L1A
- Type
- protein
- Length
- 908 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P14779
- Ligands
- HEM, OPF
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 454 | — | P14779 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- OPF · (2S)-2-[[(2S)-1-heptanoylpyrrolidin-2-yl]carbonylamino]-3-phenyl-propanoic acid · ligand · 2 copies · chains A, B
- GOL · Glycerol · additive · 4 copies · chains A, B
- DMS · Dimethyl sulfoxide · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6L1A · Crystal Structure of P450BM3 with N-enanthoyl-L-prolyl-L-phenylalanine · the same entry in another collection · chain B against B, 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 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 P14779
- Elsewhere: RCSB PDB 6L1A · PDBe 6L1A · UniProt P14779
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