3FWG: Camphor 5-monooxygenase

Ferric camphor bound Cytochrome P450cam, Arg365Leu, Glu366Gln, monoclinic crystal form. Determined by X-ray diffraction at 1.55 Å resolution. Released 3 Mar 2009.

Method: X-ray diffraction
Resolution: 1.55 Å
Organism: Pseudomonas putida
Chains: 2
Atoms: 7,561
Mol. weight: 92.97 kDa
Ligands: CAM, HEM
Released: 3 Mar 2009

Explore 3FWG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3FWG contains 58 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.

Chain A: 29 helices, 17 β-strands

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	109-119	11
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	235-251	17
α-helix	253-265	13
α-helix	268-276	9
α-helix	278-280	3
α-helix	281-291	11
β-strand	295	1	4
β-strand	297-301	5	1
β-strand	305-307	3	5
β-strand	310-312	3	5
β-strand	317-320	4	1
α-helix	322-325	4
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

Chain B: 29 helices, 17 β-strands

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	38-42	5
α-helix	43-46	4
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	108-119	12
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	253-266	14
α-helix	268-276	9
α-helix	278-280	3
α-helix	281-291	11
β-strand	295	1	10
β-strand	298-301	4	7
β-strand	305-307	3	11
β-strand	310-312	3	11
β-strand	317-319	3	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
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

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Camphor 5-monooxygenase	A, B	protein	405	Pseudomonas putida	P00183 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3FWG_1 Camphor 5-monooxygenase (chains A, B)
NLAPLPPHVPEHLVFDFDMYNPSNLSAGVQEAWAVLQESNVPDLVWTRCNGGHWIATRGQ
LIREAYEDYRHFSSECPFIPREAGEAYDFIPTSMDPPEQRQFRALANQVVGMPVVDKLEN
RIQELACSLIESLRPQGQCNFTEDYAEPFPIRIFMLLAGLPEEDIPHLKYLTDQMTRPDG
SMTFAEAKEALYDYLIPIIEQRRQKPGTDAISIVANGQVNGRPITSDEAKRMCGLLLVGG
LDTVVNFLSFSMEFLAKSPEHRQELIQRPERIPAACEELLRRFSLVADGRILTSDYEFHG
VQLKKGDQILLPQMLSGLDERENACPMHVDFSRQKVSHTTFGHGSHLCLGQHLARLQIIV
TLKEWLTRIPDFSIAPGAQIQHKSGIVSGVQALPLVWDPATTKAV

Ligands and cofactors

ID	Name	Formula	Copies
CAM	Camphor	C10 H16 O	2
HEM	Protoporphyrin IX containing FE	C34 H32 Fe N4 O4	2

Water and common crystallization additives (K, TRS) are not listed.

Primary citation

Probing the role of the proximal heme ligand in cytochrome P450cam by recombinant incorporation of selenocysteine. Aldag, C., Gromov, I.A., Garcia-Rubio, I. et al. Proc Natl Acad Sci U S A (2009) 106:5481-5486. DOI 10.1073/pnas.0810503106 · PubMed

Other PDB entries of the same protein (UniProt P00183 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4L4E 1.26 Å, Structure of cyanide and camphor bound P450cam mutant L358A/K178G
4L4F 1.29 Å, Structure of cyanide and camphor bound P450cam mutant L358A/K178G/D182N
2ZWU 1.3 Å, Crystal Structure of Camphor Soaked Ferric Cytochrome P450cam
2ZWT 1.35 Å, Crystal Structure of Ferric Cytochrome P450cam
1YRC 1.4 Å, X-ray Crystal Structure of hydrogenated Cytochrome P450cam
1RE9 1.45 Å, Crystal structure of cytochrome P450-cam with a fluorescent probe D-8-ad…
2FE6 1.5 Å, P450CAM from Pseudomonas putida reconstituted with manganic protoporphyrin IX
2H7Q 1.5 Å, Cytochrome P450cam complexed with imidazole
2ZUI 1.5 Å, Crystal Structure of Camphor-soaked Ferric Cytochrome P450cam Mutant (D297N)
3L61 1.5 Å, Crystal structure of substrate-free P450cam at 200 mM [K+]
3L63 1.5 Å, Crystal structure of camphor-bound P450cam at low [K+]
5IK1 1.53 Å, Open state of P450cam after soaking in camphor

Browse structure collections

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