3OU0: Re-refined 3CS0

re-refined 3CS0. Determined by X-ray diffraction at 3.0 Å resolution. Released 19 Jan 2011.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: Escherichia coli
Chains: 3
Atoms: 2,877
Mol. weight: 48.57 kDa
Released: 19 Jan 2011

Explore 3OU0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3OU0 contains 14 α-helices and 32 β-strands across 3 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: 13 helices, 30 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	99-103	5	1
α-helix	104-107	4
β-strand	110-116	7	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	153	1
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	221-229	9	2
β-strand	239-243	5	2
α-helix	244-257	14
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	309-313	5	5
β-strand	316-317	2	5
α-helix	321-328	8
β-strand	332	1	3
β-strand	336-343	8	5
β-strand	346-353	8	5
β-strand	355	1	4
β-strand	362-363	2	6
α-helix	365-368	4
β-strand	374-378	5	6
β-strand	385-390	6	6
β-strand	406-410	5	6
β-strand	413-414	2	6
α-helix	418-425	8
β-strand	432-438	7	6
β-strand	441-447	7	6

Chain B: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	372-374	3	2

Chain C: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
α-helix	503-504	2
β-strand	505-506	2	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Periplasmic serine endoprotease DegP	A	protein	448	Escherichia coli	P0C0V0 (AlphaFold model)
pentapeptide	B	protein	5
heptapeptide	C	protein	7

Sequence of entity 1 (A), FASTA

>3OU0_1 Periplasmic serine endoprotease DegP (chains A)
AETSSATTAQQMPSLAPMLEKVMPSVVSINVEGSTTVNTPRMPRNFQQFFGDDSPFCQEG
SPFQSSPFCQGGQGGNGGGQQQKFMALGSGVIIDADKGYVVTNNHVVDNATVIKVQLSDG
RKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMADSDALRVGDYTVAIGNPFGLGETVTSG
IVSALGRSGLNAENYENFIQTDAAINRGNAGGALVNLNGELIGINTAILAPDGGNIGIGF
AIPSNMVKNLTSQMVEYGQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAA
KAGIKAGDVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKQVNVNLELQQSSQN
QVDSSSIFNGIEGAEMSNKGKDQGVVVNNVKTGTPAAQIGLKKGDVIIGANQQAVKNIAE
LRKVLDSKPSVLALNIQRGDSTIYLLMQ

Sequence of entity 2 (B), FASTA

>3OU0_2 pentapeptide (chains B)
XXXXX

Sequence of entity 3 (C), FASTA

>3OU0_3 heptapeptide (chains C)
XXXXXXX

Primary citation

Covalent Linkage of Distinct Substrate Degrons Controls Assembly and Disassembly of DegP Proteolytic Cages. Kim, S., Grant, R.A., Sauer, R.T. Cell (2011) 145:67-78. DOI 10.1016/j.cell.2011.02.024 · 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…
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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