3MH4: Protease do

HtrA proteases are activated by a conserved mechanism that can be triggered by distinct molecular cues. Determined by X-ray diffraction at 3.1 Å resolution. Released 30 Jun 2010.

Method: X-ray diffraction
Resolution: 3.1 Å
Organism: Escherichia coli
Chains: 2
Atoms: 5,007
Mol. weight: 95.85 kDa
Released: 30 Jun 2010

Explore 3MH4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3MH4 contains 22 α-helices and 51 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: 11 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	16-22	7
α-helix	23-25	3
β-strand	26-37	12	1
α-helix	38-41	4
β-strand	80-94	15	1
β-strand	99-102	4	1
α-helix	104-107	4
β-strand	110-117	8	1
β-strand	122-131	10	1
β-strand	136-142	7	1
α-helix	149-151	3
β-strand	152	1	2
α-helix	153	1
α-helix	155-157	3
β-strand	163-168	6	2
β-strand	176-185	10	2
β-strand	199-201	3	2
β-strand	213-215	3	2
β-strand	221-226	6	2
β-strand	239-243	5	2
α-helix	244-257	14
α-helix	260-261	2
β-strand	262	1	3
α-helix	275-278	4
β-strand	288-289	2	4
β-strand	309-310	2	4
β-strand	312-313	2	5
β-strand	316-317	2	5
α-helix	322-327	6
β-strand	332	1	3
β-strand	338-340	3	6
β-strand	341-342	2	4
β-strand	347-349	3	6

Chain B: 11 helices, 29 β-strands

Element	Residues	Length	Sheet
α-helix	16-22	7
α-helix	23-25	3
β-strand	26-37	12	7
α-helix	38-40	3
β-strand	80-94	15	7
β-strand	99-102	4	7
α-helix	104-107	4
β-strand	110-116	7	7
β-strand	122-131	10	7
β-strand	136-142	7	7
β-strand	152	1	8
α-helix	155-157	3
β-strand	163-168	6	8
β-strand	176-185	10	8
β-strand	199-201	3	8
β-strand	213-215	3	8
β-strand	221-225	5	8
β-strand	239-243	5	8
α-helix	244-257	14
β-strand	263-264	2	9
β-strand	267-270	4	10
α-helix	275-279	5
β-strand	288-293	6	10
α-helix	298-302	5
β-strand	309-310	2	10
β-strand	312-313	2	11
β-strand	316-317	2	11
α-helix	321-327	7
α-helix	328-330	3
β-strand	336-340	5	11
β-strand	347-351	5	11
β-strand	353-354	2	9
β-strand	376-378	3	12
β-strand	385-387	3	12
β-strand	406-410	5	13
β-strand	413-414	2	13
α-helix	418-424	7
β-strand	434	1	14
β-strand	435-437	3	13
β-strand	445	1	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

>3MH4_1 Protease do (chains A, B)
AETSSATTAQQMPSLAPMLEKVMPSVVSINVEGSTTVNTPRMPRNFQQFFGDDSPFCQEG
SPFQSSPFCQGGQGGNGGGQQQKFMALGSGVIIDADKGYVVTNNHVVDNATVIKVQLSDG
RKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMADSDALRVGDYTVAIGNPFGLGETVTSG
IVSALGRSGLNAENYENFIQTDAAINRGNAGGALVNLNGELIGINTAILAPDGGNIGIGF
AIPSNMVKNLTSQMVEYGQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAA
KAGIKAGDVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKQVNVNLELQQSSQN
QVDSSSIFNGIEGAEMSNKGKDQGVVVNNVKTGTPAAQIGLKKGDVIIGANQQAVKNIAE
LRKVLDSKPSVLALNIQRGDSTIYLLMQRSHHHHHH

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
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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