3MH5: Protease do

HtrA proteases are activated by a conserved mechanism that can be triggered by distinct molecular cues. Determined by X-ray diffraction at 3.0 Å resolution. Released 30 Jun 2010.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: Escherichia coli
Chains: 2
Atoms: 2,922
Mol. weight: 96.22 kDa
Ligands: DFP
Released: 30 Jun 2010

Explore 3MH5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3MH5 contains 13 α-helices and 26 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: 6 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	16-22	7
α-helix	23-25	3
β-strand	26-32	7	1
β-strand	85-94	10	1
β-strand	99-103	5	1
α-helix	104-107	4
β-strand	112-116	5	1
β-strand	122-131	10	1
β-strand	136-141	6	1
α-helix	149-151	3
β-strand	152	1	2
α-helix	155-157	3
β-strand	163-168	6	2
β-strand	176-184	9	2
β-strand	199-201	3	2
β-strand	213-216	4	2
β-strand	221-226	6	2
β-strand	239-243	5	2
α-helix	244-257	14

Chain B: 7 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	16-22	7
α-helix	23-25	3
β-strand	26-37	12	3
α-helix	38-40	3
β-strand	80-94	15	3
β-strand	99-103	5	3
α-helix	104-107	4
β-strand	112-116	5	3
β-strand	122-131	10	3
β-strand	136-141	6	3
α-helix	149-151	3
β-strand	152	1	4
α-helix	155-157	3
β-strand	163-168	6	4
β-strand	176-184	9	4
β-strand	199-201	3	4
β-strand	213-216	4	4
β-strand	221-226	6	4
β-strand	239-243	5	4
α-helix	244-257	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protease do	A, B	protein	456	Escherichia coli	P0C0V0 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3MH5_1 Protease do (chains A, B)
AETSSATTAQQMPSLAPMLEKVMPSVVSINVEGSTTVNTPRMPRNFQQFFGDDSPFCQEG
SPFQSSPFCQGGQGGNGGGQQQKFMALGSGVIIDADKGYVVTNNHVVDNATVIKVQLSDG
RKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMADSDALRVGDYTVAIGNPFGLGETVTSG
IVSALGRSGLNAENYENFIQTDAAINRGNSGGALVNLNGELIGINTAILAPDGGNIGIGF
AIPSNMVKNLTSQMVEYGQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAA
KAGIKAGDVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKQVNVNLELQQSSQN
QVDSSSIFNGIEGAEMSNKGKDQGVVVNNVKTGTPAAQIGLKKGDVIIGANQQAVKNIAE
LRKVLDSKPSVLALNIQRGDSTIYLLMQRSHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
DFP	Diisopropyl phosphonate	C6 H15 O3 P	2

Primary citation

HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues. Krojer, T., Sawa, J., Huber, R. et al. Nat Struct Mol Biol (2010) 17:844-852. DOI 10.1038/nsmb.1840 · PubMed

Other PDB entries of the same protein (UniProt P0C0V0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8F0A 2.6 Å, Client-bound structure of a DegP trimer within a 12mer cage
1KY9 2.8 Å, Crystal Structure of DegP (HtrA)
3MH7 2.96 Å, HtrA proteases are activated by a conserved mechanism that can be triggered by distinct…
3CS0 3.0 Å, Crystal structure of DegP24
3OU0 3.0 Å, re-refined 3CS0
3MH4 3.1 Å, HtrA proteases are activated by a conserved mechanism that can be triggered by distinct…
8F0U 3.1 Å, Structure of a 12mer DegP cage bound to the client protein hTRF1
3MH6 3.6 Å, HtrA proteases are activated by a conserved mechanism that can be triggered by distinct…
6JJK 3.6 Å, Crystal structure of the DegP dodecamer with a modulator
3OTP 3.76 Å, Crystal structure of the DegP dodecamer with a model substrate
6JJO 4.16 Å, Crystal structure of the DegP dodecamer with a modulator
6JJL 4.2 Å, Crystal structure of the DegP dodecamer with a modulator

Browse structure collections

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