2ZWT: Ferric Cytochrome P450cam

Crystal Structure of Ferric Cytochrome P450cam. Determined by X-ray diffraction at 1.35 Å resolution. Released 17 Feb 2009.

Method: X-ray diffraction
Resolution: 1.35 Å
Organism: Pseudomonas putida
Chains: 1
Atoms: 4,697
Mol. weight: 47.65 kDa
Ligands: CAM, HEM
Released: 17 Feb 2009

Explore 2ZWT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2ZWT contains 29 α-helices and 17 β-strands across 1 chain. 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	38-43	6
α-helix	44-46	3
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	235-251	17
α-helix	253-266	14
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

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Camphor 5-monooxygenase	A	protein	415	Pseudomonas putida	P00183 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2ZWT_1 Camphor 5-monooxygenase (chains A)
MTTETIQSNANLAPLPPHVPEHLVFDFDMYNPSNLSAGVQEAWAVLQESNVPDLVWTRCN
GGHWIATRGQLIREAYEDYRHFSSECPFIPREAGEAYDFIPTSMDPPEQRQFRALANQVV
GMPVVDKLENRIQELACSLIESLRPQGQCNFTEDYAEPFPIRIFMLLAGLPEEDIPHLKY
LTDQMTRPDGSMTFAEAKEALYDYLIPIIEQRRQKPGTDAISIVANGQVNGRPITSDEAK
RMCGLLLVGGLDTVVNFLSFSMEFLAKSPEHRQELIERPERIPAACEELLRRFSLVADGR
ILTSDYEFHGVQLKKGDQILLPQMLSGLDERENACPMHVDFSRQKVSHTTFGHGSHLCLG
QHLARREIIVTLKEWLTRIPDFSIAPGAQIQHKSGIVSGVQALPLVWDPATTKAV

Ligands and cofactors

ID	Name	Formula	Copies
CAM	Camphor	C10 H16 O	1
HEM	Protoporphyrin IX containing FE	C34 H32 Fe N4 O4	1

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

Primary citation

Substrate binding induces structural changes in cytochrome P450cam. Sakurai, K., Shimada, H., Hayashi, T. et al. Acta Crystallogr Sect F Struct Biol Cryst Commun (2009) 65:80-83. DOI 10.1107/S1744309108044114 · 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
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
1QMQ 1.55 Å, Optical detection of cytochrome P450 by sensitizer-linked substrates

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