2zle

Cryo-EM structure of DegP12/OMP

Method: ELECTRON MICROSCOPY D_max: 162.7 Å Quality: GOOD

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Protease do

Escherichia coli

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 13 PDB declaration: tridecameric（13） Consistent with protein copy count	Chain A； UniProt 27–474 Chain B； UniProt 27–474 Chain C； UniProt 27–474 Chain E； UniProt 27–474 Chain F； UniProt 27–474 Chain G； UniProt 27–474 Chain H； UniProt 27–474 Chain I； UniProt 27–474 Chain J； UniProt 27–474 Chain K； UniProt 27–474 Chain L； UniProt 27–474 Chain M； UniProt 27–474	Not recorded	Outer membrane protein C × 1 （P06996）	ELECTRON MICROSCOPY cryo-EM vitrification conditions：Cryogen ETHANE；Embedded in vitreous ice using C-flat holey carbon grids (CF-2/2-4C-100, Protochip) and a Vitrobot (FEI) at 20 temperature and 100% relative humidity	Resolution 28.00 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 2ZLE	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1KY9 Crystal Structure of DegP (HtrA) Deposited 2002-02-04	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 27–474（448 aa）	Mutation：S210A Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；291 K；Isopropanol, PEG 2000 MME, Tris, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 2.80 Å R-free 0.275
1KY9 Crystal Structure of DegP (HtrA) Deposited 2002-02-04	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain B 27–474（448 aa）	Mutation：S210A Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；291 K；Isopropanol, PEG 2000 MME, Tris, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 2.80 Å R-free 0.275
3CS0 Crystal structure of DegP24 Deposited 2008-04-08	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 48 PDB declaration: 48-meric	Chain A 27–474（448 aa）	Mutation：S210A Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；292 K；PEG 550 MME, NaCl, pH 8.5, vapor diffusion, temperature 292K	Resolution 3.00 Å R-free 0.274
3MH4 HtrA proteases are activated by a conserved mechanism that can be triggered by distinct molecular cues Deposited 2010-04-07	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 27–474（448 aa）	Mutation：S210A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；293 K；12% Isopropanol, 0.1M Tris, 12% PEG 2000 MME, pH 8.5, VAPOR DIFFUSION, temperature 293K	Resolution 3.10 Å R-free 0.309
3MH4 HtrA proteases are activated by a conserved mechanism that can be triggered by distinct molecular cues Deposited 2010-04-07	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain B 27–474（448 aa）	Mutation：S210A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；293 K；12% Isopropanol, 0.1M Tris, 12% PEG 2000 MME, pH 8.5, VAPOR DIFFUSION, temperature 293K	Resolution 3.10 Å R-free 0.309
3MH5 HtrA proteases are activated by a conserved mechanism that can be triggered by distinct molecular cues Deposited 2010-04-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 27–474（448 aa）	Not recorded	DFP DIISOPROPYL PHOSPHONATE × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；293 K；12% Isopropanol, 0.1M Tris, 12% PEG 2000 MME, pH 8.5, VAPOR DIFFUSION, temperature 293K	Resolution 3.00 Å R-free 0.309
3MH5 HtrA proteases are activated by a conserved mechanism that can be triggered by distinct molecular cues Deposited 2010-04-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain B 27–474（448 aa）	Not recorded	DFP DIISOPROPYL PHOSPHONATE × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；293 K；12% Isopropanol, 0.1M Tris, 12% PEG 2000 MME, pH 8.5, VAPOR DIFFUSION, temperature 293K	Resolution 3.00 Å R-free 0.309
3MH6 HtrA proteases are activated by a conserved mechanism that can be triggered by distinct molecular cues Deposited 2010-04-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric	Chain A 27–474（448 aa）	Not recorded	DFP DIISOPROPYL PHOSPHONATE × 24	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；293 K；12% Isopropanol, 0.1M Tris, 12% PEG 2000 MME, pH 8.5, VAPOR DIFFUSION, temperature 293K	Resolution 3.60 Å R-free 0.309
3MH7 HtrA proteases are activated by a conserved mechanism that can be triggered by distinct molecular cues Deposited 2010-04-07	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 72 PDB declaration: 72-meric	Chain A 27–474（448 aa）	Mutation：S210A Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；292 K；PEG 550 MME, NaCl, pH 8.5, VAPOR DIFFUSION, temperature 292K	Resolution 2.96 Å R-free 0.249
3OTP Crystal structure of the DegP dodecamer with a model substrate Deposited 2010-09-13	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 24 PDB declaration: 24-meric	Chain A 27–474（448 aa） Fragment：UNP residues 27-474 Chain B 27–474（448 aa） Fragment：UNP residues 27-474 Chain C 27–474（448 aa） Fragment：UNP residues 27-474 Chain D 27–474（448 aa） Fragment：UNP residues 27-474 Chain E 27–474（448 aa） Fragment：UNP residues 27-474 Chain F 27–474（448 aa） Fragment：UNP residues 27-474	Mutation：S210A Mutation：S210A Mutation：S210A Mutation：S210A Mutation：S210A Mutation：S210A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 3.6；291 K；65 mM citric acid, 35 mM Bis-Tris propane, 8% PEG3350, pH 3.6, VAPOR DIFFUSION, HANGING DROP, temperature 18K, temperature 291K	Resolution 3.76 Å R-free 0.251
3OU0 re-refined 3CS0 Deposited 2010-09-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric	Chain A 27–474（448 aa） Fragment：DegP, UNP residues 27-474	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.00 Å R-free 0.229
4A8D DegP dodecamer with bound OMP Deposited 2011-11-20	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 13 PDB declaration: tridecameric	Chain A 27–474（448 aa） Fragment：DEGP Chain B 27–474（448 aa） Fragment：DEGP Chain C 27–474（448 aa） Fragment：DEGP Chain D 27–474（448 aa） Fragment：DEGP Chain E 27–474（448 aa） Fragment：DEGP Chain F 27–474（448 aa） Fragment：DEGP Chain G 27–474（448 aa） Fragment：DEGP Chain H 27–474（448 aa） Fragment：DEGP Chain I 27–474（448 aa） Fragment：DEGP Chain J 27–474（448 aa） Fragment：DEGP Chain K 27–474（448 aa） Fragment：DEGP Chain L 27–474（448 aa） Fragment：DEGP	Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 300MM NACL, 50MM HEPES- NAOH；pH 8；300MM NACL, 50MM HEPES- NAOH cryo-EM vitrification conditions Cryogen ETHANE；EMBEDDED IN VITREOUS ICE USING C-FLAT HOLEY CARBON GRIDS AND A VITROBOT AT 20C.	Resolution 28.00 Å
6JJK Crystal structure of the DegP dodecamer with a modulator Deposited 2019-02-26	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain A 35–474（440 aa） Chain B 35–474（440 aa） Chain C 35–474（440 aa） Chain D 35–474（440 aa） Chain E 35–474（440 aa） Chain F 35–474（440 aa）	Mutation：S210A Mutation：S210A Mutation：S210A Mutation：S210A Mutation：S210A Mutation：S210A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；10% PEG3350 and 0.1 M tacsimate pH 3.4	Resolution 3.60 Å R-free 0.265
6JJL Crystal structure of the DegP dodecamer with a modulator Deposited 2019-02-26	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain A 35–474（440 aa） Chain B 35–474（440 aa） Chain C 35–474（440 aa） Chain D 35–474（440 aa） Chain E 35–474（440 aa） Chain F 35–474（440 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；11% PEG3350, 0.1 M tacsimate pH 3.5	Resolution 4.20 Å R-free 0.326
6JJO Crystal structure of the DegP dodecamer with a modulator Deposited 2019-02-26	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain A 27–474（448 aa） Chain B 27–474（448 aa） Chain C 27–474（448 aa） Chain D 27–474（448 aa） Chain E 27–474（448 aa） Chain F 27–474（448 aa）	Mutation：S210A Mutation：S210A Mutation：S210A Mutation：S210A Mutation：S210A Mutation：S210A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；11% PEG3350 and 0.1 M tacsimate pH 3.5	Resolution 4.16 Å R-free 0.278
8F0A Client-bound structure of a DegP trimer within a 12mer cage Deposited 2022-11-02	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain B 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain C 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain D 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474) Chain E 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474) Chain F 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 2.60 Å
8F0U Structure of a 12mer DegP cage bound to the client protein hTRF1 Deposited 2022-11-04	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain A 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain D 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.10 Å
8F0U Structure of a 12mer DegP cage bound to the client protein hTRF1 Deposited 2022-11-04	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain D 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.10 Å
8F0U Structure of a 12mer DegP cage bound to the client protein hTRF1 Deposited 2022-11-04	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain D 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.10 Å
8F1T Structure of an 18mer DegP cage bound to the client protein hTRF1 Deposited 2022-11-06	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 54 PDB declaration: 54-meric	Chain A 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain B 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain C 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain D 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474) Chain E 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474) Chain F 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 12.10 Å
8F1T Structure of an 18mer DegP cage bound to the client protein hTRF1 Deposited 2022-11-06	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain B 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain C 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain D 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474) Chain E 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474) Chain F 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 12.10 Å
8F1T Structure of an 18mer DegP cage bound to the client protein hTRF1 Deposited 2022-11-06	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain B 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain C 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain D 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474) Chain E 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474) Chain F 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 12.10 Å
8F1U Structure of a 24mer DegP cage bound to the client protein hTRF1 Deposited 2022-11-06	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 72 PDB declaration: 72-meric	Chain A 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain B 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain C 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain D 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474) Chain E 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474) Chain F 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 13.80 Å
8F1U Structure of a 24mer DegP cage bound to the client protein hTRF1 Deposited 2022-11-06	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain B 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain C 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain D 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474) Chain E 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474) Chain F 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 13.80 Å
8F1U Structure of a 24mer DegP cage bound to the client protein hTRF1 Deposited 2022-11-06	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain B 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain C 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain D 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474) Chain E 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474) Chain F 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 13.80 Å
8F21 Structure of a 30mer DegP cage bound to the client protein hTRF1 Deposited 2022-11-06	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 90 PDB declaration: 90-meric	Chain A 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain B 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain C 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain D 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474) Chain E 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474) Chain F 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 14.10 Å
8F21 Structure of a 30mer DegP cage bound to the client protein hTRF1 Deposited 2022-11-06	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain B 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain C 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain D 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474) Chain E 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474) Chain F 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 14.10 Å
8F21 Structure of a 30mer DegP cage bound to the client protein hTRF1 Deposited 2022-11-06	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain B 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain C 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain D 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474) Chain E 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474) Chain F 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 14.10 Å
8F26 Structure of a 60mer DegP cage bound to the client protein hTRF1 Deposited 2022-11-07	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 180 PDB declaration: 180-meric	Chain A 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain D 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 9.70 Å
8F26 Structure of a 60mer DegP cage bound to the client protein hTRF1 Deposited 2022-11-07	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain D 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 9.70 Å
8F26 Structure of a 60mer DegP cage bound to the client protein hTRF1 Deposited 2022-11-07	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: pentadecameric	Chain A 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain D 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 9.70 Å
8F26 Structure of a 60mer DegP cage bound to the client protein hTRF1 Deposited 2022-11-07	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric	Chain A 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain D 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 9.70 Å
8F26 Structure of a 60mer DegP cage bound to the client protein hTRF1 Deposited 2022-11-07	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 38–385（348 aa） Fragment：protease and PDZ1 domains (UNP residues 38-385) Chain D 400–474（75 aa） Fragment：PDZ2 domain (UNP residues 400-474)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 9.70 Å

18 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	DEGP_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–448； UniProt 27–474 Author chain B； PDBConstruct 1–448； UniProt 27–474 Author chain C； PDBConstruct 1–448； UniProt 27–474 Author chain E； PDBConstruct 1–448； UniProt 27–474 Author chain F； PDBConstruct 1–448； UniProt 27–474 Author chain G； PDBConstruct 1–448； UniProt 27–474 Author chain H； PDBConstruct 1–448； UniProt 27–474 Author chain I； PDBConstruct 1–448； UniProt 27–474 Author chain J； PDBConstruct 1–448； UniProt 27–474 Author chain K； PDBConstruct 1–448； UniProt 27–474 Author chain L； PDBConstruct 1–448； UniProt 27–474 Author chain M； PDBConstruct 1–448； UniProt 27–474

Outer membrane protein C

Escherichia coli

UniProt P06996

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 13 PDB declaration: tridecameric（13） Consistent with protein copy count	Chain D； UniProt 22–367	Not recorded	Protease do × 12 （P0C0V0）	ELECTRON MICROSCOPY cryo-EM vitrification conditions：Cryogen ETHANE；Embedded in vitreous ice using C-flat holey carbon grids (CF-2/2-4C-100, Protochip) and a Vitrobot (FEI) at 20 temperature and 100% relative humidity	Resolution 28.00 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 2ZLE	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2J1N osmoporin OmpC Deposited 2006-08-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 22–367（346 aa） Chain B 22–367（346 aa） Chain C 22–367（346 aa）	Not recorded	MG MAGNESIUM ION × 3 CL CHLORIDE ION × 2 D12 DODECANE × 11	X-RAY DIFFRACTION X-ray crystallization conditions 25 MG/ML OMPC IN 25 MM TRIS-HCL (PH 8.0), 0.5 M NACL, 1.8 % (W/W) N-OCTYL-2- HYDROXYETHYLSULFOXIDE (C8HESO), 0.3 % (V/V) OCTYL-POLYOXYETHYLENE (OCTYL-POE) WERE EQUILIBRATED AGAINST A RESERVOIR SOLUTION CONTAINING 25 MM TRIS-HCL (PH 8.0), 0.5 M NACL AND 28% PEG2000.	Resolution 2.00 Å R-free 0.214
2J4U E.coli OmpC - camel Lactoferrin complex Deposited 2006-09-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain P 22–367（346 aa） Fragment：RESIDUES 22-367 Chain Q 22–367（346 aa） Fragment：RESIDUES 22-367 Chain R 22–367（346 aa） Fragment：RESIDUES 22-367	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.99 Å R-free 0.282
2J4U E.coli OmpC - camel Lactoferrin complex Deposited 2006-09-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain U 22–367（346 aa） Fragment：RESIDUES 22-367 Chain V 22–367（346 aa） Fragment：RESIDUES 22-367 Chain W 22–367（346 aa） Fragment：RESIDUES 22-367	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.99 Å R-free 0.282
3NB3 The host outer membrane proteins OmpA and OmpC are packed at specific sites in the Shigella phage Sf6 virion as structural components Deposited 2010-06-02	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 240 PDB declaration: 240-MERIC	Chain D 22–367（346 aa） Fragment：outer membrane protein C	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 10 mM Tris-HCl, pH 7.4, 10 mM MgCl2；pH 7.4；10 mM Tris-HCl, pH 7.4, 10 mM MgCl2 cryo-EM vitrification conditions Cryogen ETHANE；Vitrification was carried out with a standard cryoEM method. The sample of 4 microlitres was applied to a holey EM grid, blotted for 3-4 seconds with a Whatman #2 filter paper, and plunged into ethane slush incubated in liquid nitrogen. The grid was stored in liquid nitrogen.	Resolution 19.00 Å
3NB3 The host outer membrane proteins OmpA and OmpC are packed at specific sites in the Shigella phage Sf6 virion as structural components Deposited 2010-06-02	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain D 22–367（346 aa） Fragment：outer membrane protein C	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 10 mM Tris-HCl, pH 7.4, 10 mM MgCl2；pH 7.4；10 mM Tris-HCl, pH 7.4, 10 mM MgCl2 cryo-EM vitrification conditions Cryogen ETHANE；Vitrification was carried out with a standard cryoEM method. The sample of 4 microlitres was applied to a holey EM grid, blotted for 3-4 seconds with a Whatman #2 filter paper, and plunged into ethane slush incubated in liquid nitrogen. The grid was stored in liquid nitrogen.	Resolution 19.00 Å
3NB3 The host outer membrane proteins OmpA and OmpC are packed at specific sites in the Shigella phage Sf6 virion as structural components Deposited 2010-06-02	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain D 22–367（346 aa） Fragment：outer membrane protein C	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 10 mM Tris-HCl, pH 7.4, 10 mM MgCl2；pH 7.4；10 mM Tris-HCl, pH 7.4, 10 mM MgCl2 cryo-EM vitrification conditions Cryogen ETHANE；Vitrification was carried out with a standard cryoEM method. The sample of 4 microlitres was applied to a holey EM grid, blotted for 3-4 seconds with a Whatman #2 filter paper, and plunged into ethane slush incubated in liquid nitrogen. The grid was stored in liquid nitrogen.	Resolution 19.00 Å
3NB3 The host outer membrane proteins OmpA and OmpC are packed at specific sites in the Shigella phage Sf6 virion as structural components Deposited 2010-06-02	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 24 PDB declaration: 24-meric	Chain D 22–367（346 aa） Fragment：outer membrane protein C	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 10 mM Tris-HCl, pH 7.4, 10 mM MgCl2；pH 7.4；10 mM Tris-HCl, pH 7.4, 10 mM MgCl2 cryo-EM vitrification conditions Cryogen ETHANE；Vitrification was carried out with a standard cryoEM method. The sample of 4 microlitres was applied to a holey EM grid, blotted for 3-4 seconds with a Whatman #2 filter paper, and plunged into ethane slush incubated in liquid nitrogen. The grid was stored in liquid nitrogen.	Resolution 19.00 Å
3NB3 The host outer membrane proteins OmpA and OmpC are packed at specific sites in the Shigella phage Sf6 virion as structural components Deposited 2010-06-02	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain D 22–367（346 aa） Fragment：outer membrane protein C	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 10 mM Tris-HCl, pH 7.4, 10 mM MgCl2；pH 7.4；10 mM Tris-HCl, pH 7.4, 10 mM MgCl2 cryo-EM vitrification conditions Cryogen ETHANE；Vitrification was carried out with a standard cryoEM method. The sample of 4 microlitres was applied to a holey EM grid, blotted for 3-4 seconds with a Whatman #2 filter paper, and plunged into ethane slush incubated in liquid nitrogen. The grid was stored in liquid nitrogen.	Resolution 19.00 Å
4A8D DegP dodecamer with bound OMP Deposited 2011-11-20	Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 13 PDB declaration: tridecameric	Chain M 22–367（346 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 300MM NACL, 50MM HEPES- NAOH；pH 8；300MM NACL, 50MM HEPES- NAOH cryo-EM vitrification conditions Cryogen ETHANE；EMBEDDED IN VITREOUS ICE USING C-FLAT HOLEY CARBON GRIDS AND A VITROBOT AT 20C.	Resolution 28.00 Å
8I8R Cryo-EM Structure of OmpC3-MlaA Complex in MSP2N2 Nanodiscs Deposited 2023-02-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 22–367（346 aa） Chain B 22–367（346 aa） Chain C 22–367（346 aa）	Not recorded	KDL (2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-2-[(2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-2-carboxy-2-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-5-[[(3~{R})-3-dodecanoyloxytetradecanoyl]amino]-6-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-3-oxidanyl-5-[[(3~{R})-3-oxidanyltetradecanoyl]amino]-4-[(3~{R})-3-oxidanyltetradecanoyl]oxy-6-phosphonooxy-oxan-2-yl]methoxy]-3-phosphonooxy-4-[(3~{R})-3-tetradecanoyloxytetradecanoyl]oxy-oxan-2-yl]methoxy]-5-oxidanyl-oxan-4-yl]oxy-4,5-bis(oxidanyl)oxane-2-carboxylic acid × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8；Tris-buffered saline (TBS) buffer (20 mM Tris HCl pH 8.0, 150 mM NaCl) cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.93 Å
8I8X Cryo-EM Structure of OmpC3-MlaA-MlaC Complex in MSP2N2 Nanodiscs Deposited 2023-02-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 22–367（346 aa） Chain B 22–367（346 aa） Chain C 22–367（346 aa）	Not recorded	KDL (2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-2-[(2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-2-carboxy-2-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-5-[[(3~{R})-3-dodecanoyloxytetradecanoyl]amino]-6-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-3-oxidanyl-5-[[(3~{R})-3-oxidanyltetradecanoyl]amino]-4-[(3~{R})-3-oxidanyltetradecanoyl]oxy-6-phosphonooxy-oxan-2-yl]methoxy]-3-phosphonooxy-4-[(3~{R})-3-tetradecanoyloxytetradecanoyl]oxy-oxan-2-yl]methoxy]-5-oxidanyl-oxan-4-yl]oxy-4,5-bis(oxidanyl)oxane-2-carboxylic acid × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8；Tris-buffered saline (TBS) buffer (20 mM Tris HCl pH 8.0, 150 mM NaCl) cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.25 Å

6 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	OMPC_ECOLI
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain D； PDBConstruct 1–346； UniProt 22–367

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2zle
Deposition date deposition_date	2008-04-09
Structure title title	Cryo-EM structure of DegP12/OMP
Keywords keywords	;DegP, HtrA, protease, chaperone, PDZ, outer membrane protein, OMP, periplasm, Hydrolase, Serine protease, Stress response, Ion transport, Phage recognition, Porin, Transmembrane, Transport ;; HYDROLASE
Experimental Method method	ELECTRON MICROSCOPY

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	56.76 Å
Radius of gyration Rg (electron density) rg_electron	56.35 Å
Forward intensity I(0) i0	4163330000.00
Molecular weight molecular_weight	538040.0 kDa
Excluded volume excluded_volume	673140 Å³
Envelope volume envelope_volume	1068000 Å³
Hydration-shell volume shell_volume	150680 Å³
Envelope diameter envelope_diameter	165.4 Å
Shell Rg shell_rg	65.96 Å
Envelope Rg envelope_rg	53.39 Å
Shape Rg shape_rg	56.28 Å
Total Rg total_rg	56.79 Å
Total atoms total_atoms	37730
Residues n_residues	5098
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	162.7 Å
Rg (real space) rg_real	56.28 Å
Rg uncertainty (real space) rg_real_error	0.61 Å
I(0) (real space) i0_real	4.1630e+09
I(0) uncertainty (real space) i0_real_error	6.3880e+07
Rg (reciprocal space) rg_reciprocal	57.15 Å
I(0) (reciprocal space) i0_reciprocal	4169000000.0000
Solution quality estimate total_estimate	0.8511
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	69.7 Å
Skewness Skewness skewness	-0.068
Kurtosis Kurtosis kurtosis	-0.623
Angular range angular_range	— – 0.1400 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	496300000.0000
Real-space data points n_real_points	29
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.929; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.931; Smooth: 0.341

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Protease do
Molecular weight formula_weight	46868.9 kDa
EC 编号 ec_number	3.4.21.-
Source method src_method	man
Copy count entity_count	12

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,E,F,G,H,I,J,K,L,M
Atom count atom_count	37730

AETSSATTAQQMPSLAPMLEKVMPSVVSINVEGSTTVNTPRMPRNFQQFFGDDSPFCQEGSPFQSSPFCQGGQGGNGGGQQQKFMALGSGVIIDADKGYVVTNNHVVDNATVIKVQLSDGRKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMADSDALRVGDYTVAIGNPFGLGETVTSGIVSALGRSGLNAENYENFIQTDAAINRGNSGGALVNLNGELIGINTAILAPDGGNIGIGFAIPSNMVKNLTSQMVEYGQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAAKAGIKAGDVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKQVNVNLELQQSSQNQVDSSSIFNGIEGAEMSNKGKDQGVVVNNVKTGTPAAQIGLKKGDVIIGANQQAVKNIAELRKVLDSKPSVLALNIQRGDSTIYLLMQ

来源 Source

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	562
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Outer membrane protein C
Molecular weight formula_weight	38336.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D

AEVYNKDGNKLDLYGKVDGLHYFSDNKDVDGDQTYMRLGFKGETQVTDQLTGYGQWEYQIQGNSAENENNSWTRVAFAGLKFQDVGSFDYGRNYGVVYDVTSWTDVLPEFGGDTYGSDNFMQQRGNGFATYRNTDFFGLVDGLNFAVQYQGKNGNPSGEGFTSGVTNNGRDALRQNGDGVGGSITYDYEGFGIGGAISSSKRTDAQNTAAYIGNGDRAETYTGGLKYDANNIYLAAQYTQTYNATRVGSLGWANKAQNFEAVAQYQFDFGLRPSLAYLQSKGKNLGRGYDDEDILKYVDVGATYYFNKNMSTYVDYKINLLDDNQFTRDAGINTDNIVALGLVYQF

来源 Source

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	562
宿主生物 host_organism	Escherichia coli

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7. Fold Classification (SCOP + CATH) 36 domains

SCOP 2.08 (36 domains)

Domain ID domain_id	d2zlea1
Class class	b — All beta proteins
Fold Fold fold	b.36 — PDZ domain-like
Superfamily Superfamily superfamily	b.36.1 — PDZ domain-like
Family Family family	b.36.1.4 — HtrA-like serine proteases

Domain ID domain_id	d2zlea2
Class class	b — All beta proteins
Fold Fold fold	b.36 — PDZ domain-like
Superfamily Superfamily superfamily	b.36.1 — PDZ domain-like
Family Family family	b.36.1.4 — HtrA-like serine proteases

Domain ID domain_id	d2zlea3
Class class	b — All beta proteins
Fold Fold fold	b.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamily	b.47.1 — Trypsin-like serine proteases
Family Family family	b.47.1.1 — Prokaryotic proteases

Domain ID domain_id	d2zleb1
Class class	b — All beta proteins
Fold Fold fold	b.36 — PDZ domain-like
Superfamily Superfamily superfamily	b.36.1 — PDZ domain-like
Family Family family	b.36.1.4 — HtrA-like serine proteases

Domain ID domain_id	d2zleb2
Class class	b — All beta proteins
Fold Fold fold	b.36 — PDZ domain-like
Superfamily Superfamily superfamily	b.36.1 — PDZ domain-like
Family Family family	b.36.1.4 — HtrA-like serine proteases

Domain ID domain_id	d2zleb3
Class class	b — All beta proteins
Fold Fold fold	b.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamily	b.47.1 — Trypsin-like serine proteases
Family Family family	b.47.1.1 — Prokaryotic proteases

Domain ID domain_id	d2zlec1
Class class	b — All beta proteins
Fold Fold fold	b.36 — PDZ domain-like
Superfamily Superfamily superfamily	b.36.1 — PDZ domain-like
Family Family family	b.36.1.4 — HtrA-like serine proteases

Domain ID domain_id	d2zlec2
Class class	b — All beta proteins
Fold Fold fold	b.36 — PDZ domain-like
Superfamily Superfamily superfamily	b.36.1 — PDZ domain-like
Family Family family	b.36.1.4 — HtrA-like serine proteases

Domain ID domain_id	d2zlec3
Class class	b — All beta proteins
Fold Fold fold	b.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamily	b.47.1 — Trypsin-like serine proteases
Family Family family	b.47.1.1 — Prokaryotic proteases

Domain ID domain_id	d2zlee1
Class class	b — All beta proteins
Fold Fold fold	b.36 — PDZ domain-like
Superfamily Superfamily superfamily	b.36.1 — PDZ domain-like
Family Family family	b.36.1.4 — HtrA-like serine proteases

Domain ID domain_id	d2zlee2
Class class	b — All beta proteins
Fold Fold fold	b.36 — PDZ domain-like
Superfamily Superfamily superfamily	b.36.1 — PDZ domain-like
Family Family family	b.36.1.4 — HtrA-like serine proteases

Domain ID domain_id	d2zlee3
Class class	b — All beta proteins
Fold Fold fold	b.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamily	b.47.1 — Trypsin-like serine proteases
Family Family family	b.47.1.1 — Prokaryotic proteases

Domain ID domain_id	d2zlef1
Class class	b — All beta proteins
Fold Fold fold	b.36 — PDZ domain-like
Superfamily Superfamily superfamily	b.36.1 — PDZ domain-like
Family Family family	b.36.1.4 — HtrA-like serine proteases

Domain ID domain_id	d2zlef2
Class class	b — All beta proteins
Fold Fold fold	b.36 — PDZ domain-like
Superfamily Superfamily superfamily	b.36.1 — PDZ domain-like
Family Family family	b.36.1.4 — HtrA-like serine proteases

Domain ID domain_id	d2zlef3
Class class	b — All beta proteins
Fold Fold fold	b.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamily	b.47.1 — Trypsin-like serine proteases
Family Family family	b.47.1.1 — Prokaryotic proteases

Domain ID domain_id	d2zleg1
Class class	b — All beta proteins
Fold Fold fold	b.36 — PDZ domain-like
Superfamily Superfamily superfamily	b.36.1 — PDZ domain-like
Family Family family	b.36.1.4 — HtrA-like serine proteases

Domain ID domain_id	d2zleg2
Class class	b — All beta proteins
Fold Fold fold	b.36 — PDZ domain-like
Superfamily Superfamily superfamily	b.36.1 — PDZ domain-like
Family Family family	b.36.1.4 — HtrA-like serine proteases

Domain ID domain_id	d2zleg3
Class class	b — All beta proteins
Fold Fold fold	b.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamily	b.47.1 — Trypsin-like serine proteases
Family Family family	b.47.1.1 — Prokaryotic proteases

Domain ID domain_id	d2zleh1
Class class	b — All beta proteins
Fold Fold fold	b.36 — PDZ domain-like
Superfamily Superfamily superfamily	b.36.1 — PDZ domain-like
Family Family family	b.36.1.4 — HtrA-like serine proteases

Domain ID domain_id	d2zleh2
Class class	b — All beta proteins
Fold Fold fold	b.36 — PDZ domain-like
Superfamily Superfamily superfamily	b.36.1 — PDZ domain-like
Family Family family	b.36.1.4 — HtrA-like serine proteases

Domain ID domain_id	d2zleh3
Class class	b — All beta proteins
Fold Fold fold	b.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamily	b.47.1 — Trypsin-like serine proteases
Family Family family	b.47.1.1 — Prokaryotic proteases

Domain ID domain_id	d2zlei1
Class class	b — All beta proteins
Fold Fold fold	b.36 — PDZ domain-like
Superfamily Superfamily superfamily	b.36.1 — PDZ domain-like
Family Family family	b.36.1.4 — HtrA-like serine proteases

Domain ID domain_id	d2zlei2
Class class	b — All beta proteins
Fold Fold fold	b.36 — PDZ domain-like
Superfamily Superfamily superfamily	b.36.1 — PDZ domain-like
Family Family family	b.36.1.4 — HtrA-like serine proteases

Domain ID domain_id	d2zlei3
Class class	b — All beta proteins
Fold Fold fold	b.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamily	b.47.1 — Trypsin-like serine proteases
Family Family family	b.47.1.1 — Prokaryotic proteases

Domain ID domain_id	d2zlej1
Class class	b — All beta proteins
Fold Fold fold	b.36 — PDZ domain-like
Superfamily Superfamily superfamily	b.36.1 — PDZ domain-like
Family Family family	b.36.1.4 — HtrA-like serine proteases

Domain ID domain_id	d2zlej2
Class class	b — All beta proteins
Fold Fold fold	b.36 — PDZ domain-like
Superfamily Superfamily superfamily	b.36.1 — PDZ domain-like
Family Family family	b.36.1.4 — HtrA-like serine proteases

Domain ID domain_id	d2zlej3
Class class	b — All beta proteins
Fold Fold fold	b.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamily	b.47.1 — Trypsin-like serine proteases
Family Family family	b.47.1.1 — Prokaryotic proteases

Domain ID domain_id	d2zlek1
Class class	b — All beta proteins
Fold Fold fold	b.36 — PDZ domain-like
Superfamily Superfamily superfamily	b.36.1 — PDZ domain-like
Family Family family	b.36.1.4 — HtrA-like serine proteases

Domain ID domain_id	d2zlek2
Class class	b — All beta proteins
Fold Fold fold	b.36 — PDZ domain-like
Superfamily Superfamily superfamily	b.36.1 — PDZ domain-like
Family Family family	b.36.1.4 — HtrA-like serine proteases

Domain ID domain_id	d2zlek3
Class class	b — All beta proteins
Fold Fold fold	b.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamily	b.47.1 — Trypsin-like serine proteases
Family Family family	b.47.1.1 — Prokaryotic proteases

Domain ID domain_id	d2zlel1
Class class	b — All beta proteins
Fold Fold fold	b.36 — PDZ domain-like
Superfamily Superfamily superfamily	b.36.1 — PDZ domain-like
Family Family family	b.36.1.4 — HtrA-like serine proteases

Domain ID domain_id	d2zlel2
Class class	b — All beta proteins
Fold Fold fold	b.36 — PDZ domain-like
Superfamily Superfamily superfamily	b.36.1 — PDZ domain-like
Family Family family	b.36.1.4 — HtrA-like serine proteases

Domain ID domain_id	d2zlel3
Class class	b — All beta proteins
Fold Fold fold	b.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamily	b.47.1 — Trypsin-like serine proteases
Family Family family	b.47.1.1 — Prokaryotic proteases

Domain ID domain_id	d2zlem1
Class class	b — All beta proteins
Fold Fold fold	b.36 — PDZ domain-like
Superfamily Superfamily superfamily	b.36.1 — PDZ domain-like
Family Family family	b.36.1.4 — HtrA-like serine proteases

Domain ID domain_id	d2zlem2
Class class	b — All beta proteins
Fold Fold fold	b.36 — PDZ domain-like
Superfamily Superfamily superfamily	b.36.1 — PDZ domain-like
Family Family family	b.36.1.4 — HtrA-like serine proteases

Domain ID domain_id	d2zlem3
Class class	b — All beta proteins
Fold Fold fold	b.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamily	b.47.1 — Trypsin-like serine proteases
Family Family family	b.47.1.1 — Prokaryotic proteases

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8. Citations (1)

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Resolution resolution	28.00 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	6285

fit	/app/data/saxs_computation/zl/2zle/2zle.fit
pddf	/app/data/pr_computation/zl/2zle/2zle.pr.out
profile	/app/data/saxs_computation/zl/2zle/2zle.dat

Cryo-EM structure of DegP12/OMP

1. Protein Identity and Related Structures Protein Identity & Related Structures

Protease do

State in the Current Structure

Other States of the Same Protein in the Database

Outer membrane protein C

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 36 domains

SCOP 2.08 (36 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)