3MH6: Protease do

HtrA proteases are activated by a conserved mechanism that can be triggered by distinct molecular cues. Determined by X-ray diffraction at 3.6 Å resolution. Released 30 Jun 2010.

Method: X-ray diffraction
Resolution: 3.6 Å
Organism: Escherichia coli
Chains: 1
Atoms: 2,878
Mol. weight: 48.11 kDa
Ligands: DFP
Released: 30 Jun 2010

Explore 3MH6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3MH6 contains 11 α-helices and 36 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: 11 helices, 36 β-strands

Element	Residues	Length	Sheet
α-helix	16-22	7
α-helix	23-25	3
β-strand	26-34	9	1
β-strand	83-94	12	1
β-strand	99-101	3	1
β-strand	103	1	1
α-helix	104-107	4
β-strand	110-116	7	1
β-strand	122-131	10	1
β-strand	136-141	6	1
β-strand	152	1	2
α-helix	155-157	3
β-strand	163-168	6	2
α-helix	170-172	3
β-strand	176-187	12	2
β-strand	198-201	4	2
β-strand	213-215	3	2
β-strand	221-228	8	2
β-strand	239-243	5	2
α-helix	244-254	11
β-strand	262	1	3
β-strand	264	1	4
β-strand	267-271	5	5
α-helix	274-279	6
β-strand	288-293	6	5
α-helix	298-302	5
β-strand	309-310	2	5
β-strand	312-313	2	6
β-strand	316-317	2	6
α-helix	321-330	10
β-strand	332	1	3
β-strand	336-343	8	6
β-strand	346-353	8	6
β-strand	355	1	4
β-strand	363	1	7
β-strand	375	1	7
β-strand	376-378	3	8
β-strand	379	1	9
β-strand	382	1	9
β-strand	385-387	3	8
α-helix	397-399	3
β-strand	406-407	2	8
β-strand	409-410	2	10
β-strand	413-414	2	10
α-helix	418-427	10
β-strand	434-436	3	10
β-strand	443-445	3	10

Molecules and chains

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

Sequence of entity 1 (A), FASTA

>3MH6_1 Protease do (chains A)
AETSSATTAQQMPSLAPMLEKVMPSVVSINVEGSTTVNTPRMPRNFQQFFGDDSPFCQEG
SPFQSSPFCQGGQGGNGGGQQQKFMALGSGVIIDADKGYVVTNNHVVDNATVIKVQLSDG
RKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMADSDALRVGDYTVAIGNPFGLGETVTSG
IVSALGRSGLNAENYENFIQTDAAINRGNSGGALVNLNGELIGINTAILAPDGGNIGIGF
AIPSNMVKNLTSQMVEYGQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAA
KAGIKAGDVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKQVNVNLELQQSSQN
QVDSSSIFNGIEGAEMSNKGKDQGVVVNNVKTGTPAAQIGLKKGDVIIGANQQAVKNIAE
LRKVLDSKPSVLALNIQRGDSTIYLLMQRSHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
DFP	Diisopropyl phosphonate	C6 H15 O3 P	1

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
3MH5 3.0 Å, HtrA proteases are activated by a conserved mechanism that can be triggered by distinct…
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
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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