1PHB: Cytochrome P450-cam

Inhibitor-induced conformational change in cytochrome P450-cam. Determined by X-ray diffraction at 1.6 Å resolution. Released 31 Oct 1993.

Method: X-ray diffraction
Resolution: 1.6 Å
Organism: Pseudomonas putida
Chains: 1
Atoms: 3,505
Mol. weight: 47.55 kDa
Ligands: PFZ, HEM
Released: 31 Oct 1993

Explore 1PHB in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1PHB contains 30 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: 30 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	11-15	5
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	235-247	13
α-helix	248-252	5
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	298-301	4	1
β-strand	305-307	3	5
β-strand	310-312	3	5
β-strand	317-319	3	1
α-helix	322-324	3
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
Cytochrome P450-cam	A	protein	414	Pseudomonas putida	P00183 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1PHB_1 CYTOCHROME P450-CAM (chains A)
TTETIQSNANLAPLPPHVPEHLVFDFDMYNPSNLSAGVQEAWAVLQESNVPDLVWTRCNG
GHWIATRGQLIREAYEDYRHFSSECPFIPREAGEAYDFIPTSMDPPEQRQFRALANQVVG
MPVVDKLENRIQELACSLIESLRPQGQCNFTEDYAEPFPIRIFMLLAGLPEEDIPHLKYL
TDQMTRPDGSMTFAEAKEALYDYLIPIIEQRRQKPGTDAISIVANGQVNGRPITSDEAKR
MCGLLLVGGLDTVVNFLSFSMEFLAKSPEHRQELIERPERIPAACEELLRRFSLVADGRI
LTSDYEFHGVQLKKGDQILLPQMLSGLDERENACPMHVDFSRQKVSHTTFGHGSHLCLGQ
HLARREIIVTLKEWLTRIPDFSIAPGAQIQHKSGIVSGVQALPLVWDPATTKAV

Ligands and cofactors

ID	Name	Formula	Copies
PFZ	1-(N-imidazolyl)-2-hydroxy-2-(2,3-dichlorophenyl)octane	C17 H22 Cl2 N2 O	1
HEM	Protoporphyrin IX containing FE	C34 H32 Fe N4 O4	1

Primary citation

Inhibitor-induced conformational change in cytochrome P-450CAM. Raag, R., Li, H., Jones, B.C. et al. Biochemistry (1993) 32:4571-4578. DOI 10.1021/bi00068a013 · 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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