Crystal structure of ferrous dioxygen complex of T252A cytochrome P450cam. Determined by X-ray diffraction at 1.55 Å resolution. Released 5 Jul 2005.
Explore 2A1O in 3D Show helices and sheets RCSB PDB PDBe
2A1O contains 59 α-helices and 34 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-15 | 4 | |
| α-helix | 20-22 | 3 | |
| β-strand | 23 | 1 | 1 |
| α-helix | 34-36 | 3 | |
| α-helix | 38-42 | 5 | |
| α-helix | 43-46 | 4 | |
| β-strand | 53-56 | 4 | 1 |
| α-helix | 58-60 | 3 | |
| β-strand | 62-65 | 4 | 1 |
| α-helix | 68-76 | 9 | |
| β-strand | 81-82 | 2 | 1 |
| α-helix | 90-95 | 6 | |
| α-helix | 108-119 | 12 | |
| α-helix | 121-142 | 22 | |
| α-helix | 143-145 | 3 | |
| β-strand | 147-149 | 3 | 2 |
| α-helix | 150 | 1 | |
| α-helix | 151-155 | 5 | |
| α-helix | 157-167 | 11 | |
| α-helix | 171-173 | 3 | |
| α-helix | 174-185 | 12 | |
| α-helix | 193-213 | 21 | |
| α-helix | 219-224 | 6 | |
| β-strand | 227-228 | 2 | 3 |
| β-strand | 231-232 | 2 | 3 |
| α-helix | 233-234 | 2 | |
| α-helix | 235-250 | 16 | |
| α-helix | 252-266 | 15 | |
| α-helix | 268-276 | 9 | |
| α-helix | 278-280 | 3 | |
| α-helix | 281-291 | 11 | |
| β-strand | 295 | 1 | 4 |
| β-strand | 298-301 | 4 | 1 |
| β-strand | 305-307 | 3 | 5 |
| β-strand | 310-312 | 3 | 5 |
| β-strand | 317-319 | 3 | 1 |
| α-helix | 322-327 | 6 | |
| α-helix | 353-355 | 3 | |
| α-helix | 360-377 | 18 | |
| β-strand | 382-383 | 2 | 2 |
| α-helix | 384 | 1 | |
| β-strand | 391-392 | 2 | 6 |
| β-strand | 396 | 1 | 4 |
| β-strand | 398-399 | 2 | 6 |
| β-strand | 403-405 | 3 | 2 |
| α-helix | 408-410 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-15 | 4 | |
| α-helix | 20-22 | 3 | |
| β-strand | 23 | 1 | 7 |
| α-helix | 34-36 | 3 | |
| α-helix | 38-43 | 6 | |
| α-helix | 44-46 | 3 | |
| β-strand | 53-56 | 4 | 7 |
| α-helix | 58-60 | 3 | |
| β-strand | 62-65 | 4 | 7 |
| α-helix | 68-76 | 9 | |
| β-strand | 81-82 | 2 | 7 |
| α-helix | 90-95 | 6 | |
| α-helix | 107-119 | 13 | |
| α-helix | 121-142 | 22 | |
| α-helix | 143-145 | 3 | |
| β-strand | 147-149 | 3 | 8 |
| α-helix | 150 | 1 | |
| α-helix | 151-155 | 5 | |
| α-helix | 157-167 | 11 | |
| α-helix | 171-173 | 3 | |
| α-helix | 174-185 | 12 | |
| α-helix | 193-213 | 21 | |
| α-helix | 219-224 | 6 | |
| β-strand | 227-228 | 2 | 9 |
| β-strand | 231-232 | 2 | 9 |
| α-helix | 233-234 | 2 | |
| α-helix | 235-250 | 16 | |
| α-helix | 252-266 | 15 | |
| α-helix | 268-276 | 9 | |
| α-helix | 278-280 | 3 | |
| α-helix | 281-291 | 11 | |
| β-strand | 295 | 1 | 10 |
| β-strand | 297-301 | 5 | 7 |
| β-strand | 305-307 | 3 | 11 |
| β-strand | 310-312 | 3 | 11 |
| β-strand | 317-320 | 4 | 7 |
| α-helix | 322-325 | 4 | |
| α-helix | 353-355 | 3 | |
| α-helix | 360-377 | 18 | |
| β-strand | 382-383 | 2 | 8 |
| α-helix | 384 | 1 | |
| α-helix | 389-390 | 2 | |
| β-strand | 391-392 | 2 | 12 |
| β-strand | 396 | 1 | 10 |
| β-strand | 398-399 | 2 | 12 |
| β-strand | 403-405 | 3 | 8 |
| α-helix | 408-410 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cytochrome P450-cam | A, B | protein | 415 | Pseudomonas putida | P00183 (AlphaFold model) |
>2A1O_1 Cytochrome P450-cam (chains A, B) MTTETIQSNANLAPLPPHVPEHLVFDFDMYNPSNLSAGVQEAWAVLQESNVPDLVWTRCN GGHWIATRGQLIREAYEDYRHFSSECPFIPREAGEAYDFIPTSMDPPEQRQFRALANQVV GMPVVDKLENRIQELACSLIESLRPQGQCNFTEDYAEPFPIRIFMLLAGLPEEDIPHLKY LTDQMTRPDGSMTFAEAKEALYDYLIPIIEQRRQKPGTDAISIVANGQVNGRPITSDEAK RMCGLLLVGGLDAVVNFLSFSMEFLAKSPEHRQELIERPERIPAACEELLRRFSLVADGR ILTSDYEFHGVQLKKGDQILLPQMLSGLDERENAAPMHVDFSRQKVSHTTFGHGSHLCLG QHLARREIIVTLKEWLTRIPDFSIAPGAQIQHKSGIVSGVQALPLVWDPATTKAV
| ID | Name | Formula | Copies |
|---|---|---|---|
| HEM | Protoporphyrin IX containing FE | C34 H32 Fe N4 O4 | 2 |
| OXY | Oxygen molecule | O2 | 2 |
| CAM | Camphor | C10 H16 O | 2 |
Water and common crystallization additives (TRS, K) are not listed.
Crystallographic study on the dioxygen complex of wild-type and mutant cytochrome P450cam. Implications for the dioxygen activation mechanism. Nagano, S., Poulos, T.L. J Biol Chem (2005) 280:31659-31663. DOI 10.1074/jbc.M505261200 · PubMed
Other PDB entries of the same protein (UniProt P00183 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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