3mt6

Structure of ClpP from Escherichia coli in complex with ADEP1

Method: X-RAY DIFFRACTION D_max: 195.2 Å Quality: REASONABLE

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

ATP-dependent Clp protease proteolytic subunit

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 × 28 PDB declaration: 28-meric（28） Consistent with protein copy count	Chain O； UniProt 1–207 Chain P； UniProt 1–207 Chain Q； UniProt 1–207 Chain R； UniProt 1–207 Chain S； UniProt 1–207 Chain T； UniProt 1–207 Chain U； UniProt 1–207 Chain V； UniProt 1–207 Chain W； UniProt 1–207 Chain X； UniProt 1–207 Chain Y； UniProt 1–207 Chain Z； UniProt 1–207 Chain a； UniProt 1–207 Chain b； UniProt 1–207	Not recorded	ACYLDEPSIPEPTIDE 1 × 14 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 27	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5；295.15 K；25-35% (v/v) MPD and 0.1 M sodium acetate at pH 5, VAPOR DIFFUSION, HANGING DROP, temperature 295.15K	Resolution 1.90 Å R-free 0.204
2	Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric（28） Consistent with protein copy count	Chain A； UniProt 1–207 Chain B； UniProt 1–207 Chain C； UniProt 1–207 Chain D； UniProt 1–207 Chain E； UniProt 1–207 Chain F； UniProt 1–207 Chain G； UniProt 1–207 Chain H； UniProt 1–207 Chain I； UniProt 1–207 Chain J； UniProt 1–207 Chain K； UniProt 1–207 Chain L； UniProt 1–207 Chain M； UniProt 1–207 Chain N； UniProt 1–207	Not recorded	ACYLDEPSIPEPTIDE 1 × 14 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 28	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5；295.15 K；25-35% (v/v) MPD and 0.1 M sodium acetate at pH 5, VAPOR DIFFUSION, HANGING DROP, temperature 295.15K	Resolution 1.90 Å R-free 0.204

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 3MT6	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1TYF THE STRUCTURE OF CLPP AT 2.3 ANGSTROM RESOLUTION SUGGESTS A MODEL FOR ATP-DEPENDENT PROTEOLYSIS Deposited 1997-10-13	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric	Chain A 15–207（193 aa） Chain B 15–207（193 aa） Chain C 15–207（193 aa） Chain D 15–207（193 aa） Chain E 15–207（193 aa） Chain F 15–207（193 aa） Chain G 15–207（193 aa） Chain H 15–207（193 aa） Chain I 15–207（193 aa） Chain J 15–207（193 aa） Chain K 15–207（193 aa） Chain L 15–207（193 aa） Chain M 15–207（193 aa） Chain N 15–207（193 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å R-free 0.292
1YG6 ClpP Deposited 2005-01-04	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric	Chain A 15–207（193 aa） Chain B 15–207（193 aa） Chain C 15–207（193 aa） Chain D 15–207（193 aa） Chain E 15–207（193 aa） Chain F 15–207（193 aa） Chain G 15–207（193 aa） Chain H 15–207（193 aa） Chain I 15–207（193 aa） Chain J 15–207（193 aa） Chain K 15–207（193 aa） Chain L 15–207（193 aa） Chain M 15–207（193 aa） Chain N 15–207（193 aa）	Not recorded	MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 14	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.2；298 K；mpd, mes, pH 6.2, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 1.90 Å R-free 0.251
2FZS Crystal structure of E. coli ClpP with a Peptide Chloromethyl Ketone Covalently Bound at the Active Site Deposited 2006-02-10	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric	Chain A 15–207（193 aa） Chain B 15–207（193 aa） Chain C 15–207（193 aa） Chain D 15–207（193 aa） Chain E 15–207（193 aa） Chain F 15–207（193 aa） Chain G 15–207（193 aa） Chain H 15–207（193 aa） Chain I 15–207（193 aa） Chain J 15–207（193 aa） Chain K 15–207（193 aa） Chain L 15–207（193 aa） Chain M 15–207（193 aa） Chain N 15–207（193 aa）	Not recorded	CMQ N~2~-[(BENZYLOXY)CARBONYL]-N-[(1S,2S)-2-HYDROXY-1-(4-HYDROXYBENZYL)PROPYL]-L-LEUCINAMIDE × 14 PGE TRIETHYLENE GLYCOL × 15 GOL GLYCEROL × 11	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；298 K；0.1M tri-sodium citrate, 0.15M ammonium acetate, 30% PEG 4000 , pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 1.90 Å R-free 0.233
3HLN Crystal structure of ClpP A153C mutant with inter-heptamer disulfide bonds Deposited 2009-05-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric	Chain A 15–207（193 aa） Fragment：UNP residues 15-207 Chain B 15–207（193 aa） Fragment：UNP residues 15-207 Chain C 15–207（193 aa） Fragment：UNP residues 15-207 Chain D 15–207（193 aa） Fragment：UNP residues 15-207 Chain E 15–207（193 aa） Fragment：UNP residues 15-207 Chain F 15–207（193 aa） Fragment：UNP residues 15-207 Chain G 15–207（193 aa） Fragment：UNP residues 15-207 Chain H 15–207（193 aa） Fragment：UNP residues 15-207 Chain I 15–207（193 aa） Fragment：UNP residues 15-207 Chain J 15–207（193 aa） Fragment：UNP residues 15-207 Chain K 15–207（193 aa） Fragment：UNP residues 15-207 Chain L 15–207（193 aa） Fragment：UNP residues 15-207 Chain M 15–207（193 aa） Fragment：UNP residues 15-207 Chain N 15–207（193 aa） Fragment：UNP residues 15-207	Mutation：A153C Mutation：A153C Mutation：A153C Mutation：A153C Mutation：A153C Mutation：A153C Mutation：A153C Mutation：A153C Mutation：A153C Mutation：A153C Mutation：A153C Mutation：A153C Mutation：A153C Mutation：A153C	CA CALCIUM ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.6；293 K；1 M 1,6-hexanediol, 0.1 M Sodium acetate pH 4.6, 10 mM CoCl2, 100 mM CaCl2, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 3.20 Å R-free 0.253
3HLN Crystal structure of ClpP A153C mutant with inter-heptamer disulfide bonds Deposited 2009-05-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric	Chain 1 15–207（193 aa） Fragment：UNP residues 15-207 Chain 2 15–207（193 aa） Fragment：UNP residues 15-207 Chain O 15–207（193 aa） Fragment：UNP residues 15-207 Chain P 15–207（193 aa） Fragment：UNP residues 15-207 Chain Q 15–207（193 aa） Fragment：UNP residues 15-207 Chain R 15–207（193 aa） Fragment：UNP residues 15-207 Chain S 15–207（193 aa） Fragment：UNP residues 15-207 Chain T 15–207（193 aa） Fragment：UNP residues 15-207 Chain U 15–207（193 aa） Fragment：UNP residues 15-207 Chain V 15–207（193 aa） Fragment：UNP residues 15-207 Chain W 15–207（193 aa） Fragment：UNP residues 15-207 Chain X 15–207（193 aa） Fragment：UNP residues 15-207 Chain Y 15–207（193 aa） Fragment：UNP residues 15-207 Chain Z 15–207（193 aa） Fragment：UNP residues 15-207	Mutation：A153C Mutation：A153C Mutation：A153C Mutation：A153C Mutation：A153C Mutation：A153C Mutation：A153C Mutation：A153C Mutation：A153C Mutation：A153C Mutation：A153C Mutation：A153C Mutation：A153C Mutation：A153C	CA CALCIUM ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.6；293 K；1 M 1,6-hexanediol, 0.1 M Sodium acetate pH 4.6, 10 mM CoCl2, 100 mM CaCl2, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 3.20 Å R-free 0.253
6NB1 Crystal structure of Escherichia coli ClpP protease complexed with small molecule activator, ACP1-06 Deposited 2018-12-06	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric	Chain A 1–207（207 aa） Chain B 1–207（207 aa） Chain C 1–207（207 aa） Chain D 1–207（207 aa） Chain E 1–207（207 aa） Chain F 1–207（207 aa） Chain G 1–207（207 aa） Chain H 1–207（207 aa） Chain I 1–207（207 aa） Chain J 1–207（207 aa） Chain K 1–207（207 aa） Chain L 1–207（207 aa） Chain M 1–207（207 aa） Chain N 1–207（207 aa）	Not recorded	KHS N-{2-[(2-chlorophenyl)sulfanyl]ethyl}-2-methyl-2-{[5-(trifluoromethyl)pyridin-2-yl]sulfonyl}propanamide × 14 GOL GLYCEROL × 14	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；294 K；51-63% MPD 0.1 M sodium acetate pH 5.0	Resolution 1.90 Å R-free 0.244
6WR2 ClpP and ClpX IGF loop in ClpX-ClpP complex bound to ssrA tagged GFP Deposited 2020-04-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain H 16–207（192 aa） Chain I 16–207（192 aa） Chain J 16–207（192 aa） Chain K 16–207（192 aa） Chain L 16–207（192 aa） Chain M 16–207（192 aa） Chain N 16–207（192 aa） Chain h 16–207（192 aa） Chain i 16–207（192 aa） Chain j 16–207（192 aa） Chain k 16–207（192 aa） Chain l 16–207（192 aa） Chain m 16–207（192 aa） Chain n 16–207（192 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.88 Å
6WRF ClpX-ClpP complex bound to GFP-ssrA, recognition complex Deposited 2020-04-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric	Chain H 16–207（192 aa） Chain I 16–207（192 aa） Chain J 16–207（192 aa） Chain K 16–207（192 aa） Chain L 16–207（192 aa） Chain M 16–207（192 aa） Chain N 16–207（192 aa）	Not recorded	AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.14 Å
6WSG ClpX-ClpP complex bound to ssrA-tagged GFP, intermediate complex Deposited 2020-04-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric	Chain H 16–207（192 aa） Fragment：UNP residues 16-207 Chain I 16–207（192 aa） Fragment：UNP residues 16-207 Chain J 16–207（192 aa） Fragment：UNP residues 16-207 Chain K 16–207（192 aa） Fragment：UNP residues 16-207 Chain L 16–207（192 aa） Fragment：UNP residues 16-207 Chain M 16–207（192 aa） Fragment：UNP residues 16-207 Chain N 16–207（192 aa） Fragment：UNP residues 16-207	Not recorded	AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.16 Å
7MK5 Crystal structure of Escherichia coli ClpP covalently inhibited by clipibicyclene Deposited 2021-04-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric	Chain A 15–207（193 aa） Chain B 15–207（193 aa） Chain C 15–207（193 aa） Chain D 15–207（193 aa） Chain E 15–207（193 aa） Chain F 15–207（193 aa） Chain G 15–207（193 aa） Chain H 15–207（193 aa） Chain I 15–207（193 aa） Chain J 15–207（193 aa） Chain K 15–207（193 aa） Chain L 15–207（193 aa） Chain M 15–207（193 aa） Chain N 15–207（193 aa）	Not recorded	MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 25 ACT ACETATE ION × 6 ZGV 4-[(1E)-3-{[(2E,4E,6E,8S)-8-hydroxy-4-methyldeca-2,4,6-trienoyl]amino}-3-oxoprop-1-en-1-yl]azete-1(2H)-carboxylic acid × 14	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；293 K；0.1 M sodium acetate, 30% MPD	Resolution 2.95 Å R-free 0.248
7MK5 Crystal structure of Escherichia coli ClpP covalently inhibited by clipibicyclene Deposited 2021-04-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric	Chain O 15–207（193 aa） Chain P 15–207（193 aa） Chain Q 15–207（193 aa） Chain R 15–207（193 aa） Chain S 15–207（193 aa） Chain T 15–207（193 aa） Chain U 15–207（193 aa） Chain V 15–207（193 aa） Chain W 15–207（193 aa） Chain X 15–207（193 aa） Chain Y 15–207（193 aa） Chain Z 15–207（193 aa） Chain a 15–207（193 aa） Chain b 15–207（193 aa）	Not recorded	MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 25 ACT ACETATE ION × 4 ZGV 4-[(1E)-3-{[(2E,4E,6E,8S)-8-hydroxy-4-methyldeca-2,4,6-trienoyl]amino}-3-oxoprop-1-en-1-yl]azete-1(2H)-carboxylic acid × 14	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；293 K；0.1 M sodium acetate, 30% MPD	Resolution 2.95 Å R-free 0.248
8E7V Cryo-EM structure of substrate-free DNClpX.ClpP from singly capped particles Deposited 2022-08-24	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain H 16–207（192 aa） Fragment：UNP residues 16-207 Chain I 16–207（192 aa） Fragment：UNP residues 16-207 Chain J 16–207（192 aa） Fragment：UNP residues 16-207 Chain K 16–207（192 aa） Fragment：UNP residues 16-207 Chain L 16–207（192 aa） Fragment：UNP residues 16-207 Chain M 16–207（192 aa） Fragment：UNP residues 16-207 Chain N 16–207（192 aa） Fragment：UNP residues 16-207 Chain h 16–207（192 aa） Fragment：UNP residues 16-207 Chain i 16–207（192 aa） Fragment：UNP residues 16-207 Chain j 16–207（192 aa） Fragment：UNP residues 16-207 Chain k 16–207（192 aa） Fragment：UNP residues 16-207 Chain l 16–207（192 aa） Fragment：UNP residues 16-207 Chain m 16–207（192 aa） Fragment：UNP residues 16-207 Chain n 16–207（192 aa） Fragment：UNP residues 16-207	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
8E8Q Cryo-EM structure of substrate-free DNClpX.ClpP Deposited 2022-08-25	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain H 16–207（192 aa） Fragment：UNP residues 16-207 Chain I 16–207（192 aa） Fragment：UNP residues 16-207 Chain J 16–207（192 aa） Fragment：UNP residues 16-207 Chain K 16–207（192 aa） Fragment：UNP residues 16-207 Chain L 16–207（192 aa） Fragment：UNP residues 16-207 Chain M 16–207（192 aa） Fragment：UNP residues 16-207 Chain N 16–207（192 aa） Fragment：UNP residues 16-207 Chain h 16–207（192 aa） Fragment：UNP residues 16-207 Chain i 16–207（192 aa） Fragment：UNP residues 16-207 Chain j 16–207（192 aa） Fragment：UNP residues 16-207 Chain k 16–207（192 aa） Fragment：UNP residues 16-207 Chain l 16–207（192 aa） Fragment：UNP residues 16-207 Chain m 16–207（192 aa） Fragment：UNP residues 16-207 Chain n 16–207（192 aa） Fragment：UNP residues 16-207	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.12 Å
8E91 Cryo-EM structure of substrate-free ClpX.ClpP Deposited 2022-08-26	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain H 16–207（192 aa） Fragment：UNP residues 16-207 Chain I 16–207（192 aa） Fragment：UNP residues 16-207 Chain J 16–207（192 aa） Fragment：UNP residues 16-207 Chain K 16–207（192 aa） Fragment：UNP residues 16-207 Chain L 16–207（192 aa） Fragment：UNP residues 16-207 Chain M 16–207（192 aa） Fragment：UNP residues 16-207 Chain N 16–207（192 aa） Fragment：UNP residues 16-207 Chain h 16–207（192 aa） Fragment：UNP residues 16-207 Chain i 16–207（192 aa） Fragment：UNP residues 16-207 Chain j 16–207（192 aa） Fragment：UNP residues 16-207 Chain k 16–207（192 aa） Fragment：UNP residues 16-207 Chain l 16–207（192 aa） Fragment：UNP residues 16-207 Chain m 16–207（192 aa） Fragment：UNP residues 16-207 Chain n 16–207（192 aa） Fragment：UNP residues 16-207	Not recorded	AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.57 Å
8ET3 Cryo-EM structure of a delivery complex containing the SspB adaptor, an ssrA-tagged substrate, and the AAA+ ClpXP protease Deposited 2022-10-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric	Chain H 16–207（192 aa） Fragment：UNP residues 16-207 Chain I 16–207（192 aa） Fragment：UNP residues 16-207 Chain J 16–207（192 aa） Fragment：UNP residues 16-207 Chain K 16–207（192 aa） Fragment：UNP residues 16-207 Chain L 16–207（192 aa） Fragment：UNP residues 16-207 Chain M 16–207（192 aa） Fragment：UNP residues 16-207 Chain N 16–207（192 aa） Fragment：UNP residues 16-207	Not recorded	AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å
8V9R Cryo-EM Structure of a Proteolytic ClpXP AAA+ Machine Poised to Unfold a Branched-Degron DHFR-ssrA Substrate Bound with MTX Deposited 2023-12-09	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 21 PDB declaration: 21-meric	Chain h 16–207（192 aa） Fragment：UNP residues 16-207 Chain i 16–207（192 aa） Fragment：UNP residues 16-207 Chain j 16–207（192 aa） Fragment：UNP residues 16-207 Chain k 16–207（192 aa） Fragment：UNP residues 16-207 Chain l 16–207（192 aa） Fragment：UNP residues 16-207 Chain m 16–207（192 aa） Fragment：UNP residues 16-207 Chain n 16–207（192 aa） Fragment：UNP residues 16-207 Chain p 16–207（192 aa） Fragment：UNP residues 16-207 Chain q 16–207（192 aa） Fragment：UNP residues 16-207 Chain r 16–207（192 aa） Fragment：UNP residues 16-207 Chain s 16–207（192 aa） Fragment：UNP residues 16-207 Chain t 16–207（192 aa） Fragment：UNP residues 16-207 Chain u 16–207（192 aa） Fragment：UNP residues 16-207 Chain v 16–207（192 aa） Fragment：UNP residues 16-207	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 3 MTX METHOTREXATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
9C87 Cryo-EM Structure of a Proteolytic ClpXP AAA+ Machine Poised to Unfold a Linear-Degron DHFR-ssrA Substrate Bound with MTX Deposited 2024-06-12	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 21 PDB declaration: 21-meric	Chain h 16–207（192 aa） Fragment：UNP residues 16-207 Chain i 16–207（192 aa） Fragment：UNP residues 16-207 Chain j 16–207（192 aa） Fragment：UNP residues 16-207 Chain k 16–207（192 aa） Fragment：UNP residues 16-207 Chain l 16–207（192 aa） Fragment：UNP residues 16-207 Chain m 16–207（192 aa） Fragment：UNP residues 16-207 Chain n 16–207（192 aa） Fragment：UNP residues 16-207 Chain p 16–207（192 aa） Fragment：UNP residues 16-207 Chain q 16–207（192 aa） Fragment：UNP residues 16-207 Chain r 16–207（192 aa） Fragment：UNP residues 16-207 Chain s 16–207（192 aa） Fragment：UNP residues 16-207 Chain t 16–207（192 aa） Fragment：UNP residues 16-207 Chain u 16–207（192 aa） Fragment：UNP residues 16-207 Chain v 16–207（192 aa） Fragment：UNP residues 16-207	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 3 MTX METHOTREXATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å
9C88 Cryo-EM Structure of a Proteolytic ClpXP AAA+ Machine Translocating a Portion of a Branched-Degron DHFR Substrate Deposited 2024-06-12	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 21 PDB declaration: 21-meric	Chain h 16–207（192 aa） Fragment：UNP residues 16-207 Chain i 16–207（192 aa） Fragment：UNP residues 16-207 Chain j 16–207（192 aa） Fragment：UNP residues 16-207 Chain k 16–207（192 aa） Fragment：UNP residues 16-207 Chain l 16–207（192 aa） Fragment：UNP residues 16-207 Chain m 16–207（192 aa） Fragment：UNP residues 16-207 Chain n 16–207（192 aa） Fragment：UNP residues 16-207 Chain p 16–207（192 aa） Fragment：UNP residues 16-207 Chain q 16–207（192 aa） Fragment：UNP residues 16-207 Chain r 16–207（192 aa） Fragment：UNP residues 16-207 Chain s 16–207（192 aa） Fragment：UNP residues 16-207 Chain t 16–207（192 aa） Fragment：UNP residues 16-207 Chain u 16–207（192 aa） Fragment：UNP residues 16-207 Chain v 16–207（192 aa） Fragment：UNP residues 16-207	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.60 Å
9PIO Cryo-EM structure of the ClpXP AAA+ protease bound to lambdaO-tagged Arc in a recognition complex Deposited 2025-07-10	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 21 PDB declaration: 21-meric	Chain H 16–207（192 aa） Fragment：UNP residues 16-207 Chain I 16–207（192 aa） Fragment：UNP residues 16-207 Chain J 16–207（192 aa） Fragment：UNP residues 16-207 Chain K 16–207（192 aa） Fragment：UNP residues 16-207 Chain L 16–207（192 aa） Fragment：UNP residues 16-207 Chain M 16–207（192 aa） Fragment：UNP residues 16-207 Chain N 16–207（192 aa） Fragment：UNP residues 16-207 Chain O 16–207（192 aa） Fragment：UNP residues 16-207 Chain P 16–207（192 aa） Fragment：UNP residues 16-207 Chain Q 16–207（192 aa） Fragment：UNP residues 16-207 Chain R 16–207（192 aa） Fragment：UNP residues 16-207 Chain S 16–207（192 aa） Fragment：UNP residues 16-207 Chain T 16–207（192 aa） Fragment：UNP residues 16-207 Chain U 16–207（192 aa） Fragment：UNP residues 16-207	Not recorded	AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.61 Å
9PJD Cryo-EM structure of the ClpXP AAA+ protease bound to an unidentified portion of lambdaO-tagged Arc substrate within a translocation complex Deposited 2025-07-13	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 20 PDB declaration: 21-meric	Chain H 16–207（192 aa） Fragment：UNP residues 16-207 Chain I 16–207（192 aa） Fragment：UNP residues 16-207 Chain J 16–207（192 aa） Fragment：UNP residues 16-207 Chain K 16–207（192 aa） Fragment：UNP residues 16-207 Chain L 16–207（192 aa） Fragment：UNP residues 16-207 Chain M 16–207（192 aa） Fragment：UNP residues 16-207 Chain N 16–207（192 aa） Fragment：UNP residues 16-207 Chain O 16–207（192 aa） Fragment：UNP residues 16-207 Chain P 16–207（192 aa） Fragment：UNP residues 16-207 Chain Q 16–207（192 aa） Fragment：UNP residues 16-207 Chain R 16–207（192 aa） Fragment：UNP residues 16-207 Chain S 16–207（192 aa） Fragment：UNP residues 16-207 Chain T 16–207（192 aa） Fragment：UNP residues 16-207 Chain U 16–207（192 aa） Fragment：UNP residues 16-207	Not recorded	AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 6 MG MAGNESIUM ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.67 Å

18 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CLPP_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–207； UniProt 1–207 Author chain B； PDBConstruct 1–207； UniProt 1–207 Author chain C； PDBConstruct 1–207； UniProt 1–207 Author chain D； PDBConstruct 1–207； UniProt 1–207 Author chain E； PDBConstruct 1–207； UniProt 1–207 Author chain F； PDBConstruct 1–207； UniProt 1–207 Author chain G； PDBConstruct 1–207； UniProt 1–207 Author chain H； PDBConstruct 1–207； UniProt 1–207 Author chain I； PDBConstruct 1–207； UniProt 1–207 Author chain J； PDBConstruct 1–207； UniProt 1–207 Author chain K； PDBConstruct 1–207； UniProt 1–207 Author chain L； PDBConstruct 1–207； UniProt 1–207 Author chain M； PDBConstruct 1–207； UniProt 1–207 Author chain N； PDBConstruct 1–207； UniProt 1–207 Author chain O； PDBConstruct 1–207； UniProt 1–207 Author chain P； PDBConstruct 1–207； UniProt 1–207 Author chain Q； PDBConstruct 1–207； UniProt 1–207 Author chain R； PDBConstruct 1–207； UniProt 1–207 Author chain S； PDBConstruct 1–207； UniProt 1–207 Author chain T； PDBConstruct 1–207； UniProt 1–207 Author chain U； PDBConstruct 1–207； UniProt 1–207 Author chain V； PDBConstruct 1–207； UniProt 1–207 Author chain W； PDBConstruct 1–207； UniProt 1–207 Author chain X； PDBConstruct 1–207； UniProt 1–207 Author chain Y； PDBConstruct 1–207； UniProt 1–207 Author chain Z； PDBConstruct 1–207； UniProt 1–207 Author chain a； PDBConstruct 1–207； UniProt 1–207 Author chain b； PDBConstruct 1–207； UniProt 1–207

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	3mt6
Deposition date deposition_date	2010-04-30
Structure title title	Structure of ClpP from Escherichia coli in complex with ADEP1
Keywords keywords	ENDOPEPTIDASE CLP, CASEINOLYTIC PROTEASE, PROTEASE TI, ACYPDEPSIPEPTIDE ANTIBIOTICS, HYDROLASE-ANTIBIOTIC COMPLEX; HYDROLASE/ANTIBIOTIC
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	65.73 Å
Radius of gyration Rg (electron density) rg_electron	66.00 Å
Forward intensity I(0) i0	4953640000.00
Molecular weight molecular_weight	609270.0 kDa
Excluded volume excluded_volume	768840 Å³
Envelope volume envelope_volume	1121200 Å³
Hydration-shell volume shell_volume	141950 Å³
Envelope diameter envelope_diameter	209.2 Å
Shell Rg shell_rg	66.22 Å
Envelope Rg envelope_rg	63.72 Å
Shape Rg shape_rg	66.02 Å
Total Rg total_rg	65.93 Å
Total atoms total_atoms	42681
Residues n_residues	5344
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	195.2 Å
Rg (real space) rg_real	65.99 Å
Rg uncertainty (real space) rg_real_error	1.12 Å
I(0) (real space) i0_real	4.9540e+09
I(0) uncertainty (real space) i0_real_error	9.8250e+07
Rg (reciprocal space) rg_reciprocal	65.43 Å
I(0) (reciprocal space) i0_reciprocal	4948000000.0000
Solution quality estimate total_estimate	0.5759
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	65.1 Å
Skewness Skewness skewness	0.418
Kurtosis Kurtosis kurtosis	-0.524
Angular range angular_range	— – 0.1200 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	4443000000.0000
Real-space data points n_real_points	25
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.815; Stabil: 1.000; Sysdev: 0.013; Positv: 1.000; Valcen: 0.997; Smooth: 0.001

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	ATP-dependent Clp protease proteolytic subunit
Molecular weight formula_weight	23212.7 kDa
EC 编号 ec_number	3.4.21.92
Source method src_method	man
Copy count entity_count	28

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	R,S,T,U,O,P,Q,Y,Z,a,b,V,W,X,M,L,K,J,I,H,N,F,E,D,C,B,A,G
Atom count atom_count	46463

MSYSGERDNFAPHMALVPMVIEQTSRGERSFDIYSRLLKERVIFLTGQVEDHMANLIVAQMLFLEAENPEKDIYLYINSPGGVITAGMSIYDTMQFIKPDVSTICMGQAASMGAFLLTAGAKGKRFCLPNSRVMIHQPLGGYQGQATDIEIHAREILKVKGRMNELMALHTGQSLEQIERDTERDRFLSAPEAVEYGLVDSILTHRN

来源 Source

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	83333
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	ACYLDEPSIPEPTIDE 1
Molecular weight formula_weight	736.9 kDa
Source method src_method	nat
Copy count entity_count	28

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	1,2,c,d,e,f,g,h,i,j,k,l,m,n,o,p,q,r,s,t,v,w,x,y,z,3,4,u

XFSPAAP

Entity 3 Entity 3 non-polymer

Description description	(4S)-2-METHYL-2,4-PENTANEDIOL
Molecular weight formula_weight	118.2 kDa
Source method src_method	syn
Copy count entity_count	55

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	3591

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7. Fold Classification (SCOP + CATH) 54 domains

SCOP 2.08 (26 domains)

Domain ID domain_id	d3mt6a_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.14 — ClpP/crotonase
Superfamily Superfamily superfamily	c.14.1 — ClpP/crotonase
Family Family family	c.14.1.1 — Clp protease, ClpP subunit

Domain ID domain_id	d3mt6b_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.14 — ClpP/crotonase
Superfamily Superfamily superfamily	c.14.1 — ClpP/crotonase
Family Family family	c.14.1.1 — Clp protease, ClpP subunit

Domain ID domain_id	d3mt6c_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.14 — ClpP/crotonase
Superfamily Superfamily superfamily	c.14.1 — ClpP/crotonase
Family Family family	c.14.1.1 — Clp protease, ClpP subunit

Domain ID domain_id	d3mt6d_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.14 — ClpP/crotonase
Superfamily Superfamily superfamily	c.14.1 — ClpP/crotonase
Family Family family	c.14.1.1 — Clp protease, ClpP subunit

Domain ID domain_id	d3mt6e_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.14 — ClpP/crotonase
Superfamily Superfamily superfamily	c.14.1 — ClpP/crotonase
Family Family family	c.14.1.1 — Clp protease, ClpP subunit

Domain ID domain_id	d3mt6f_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.14 — ClpP/crotonase
Superfamily Superfamily superfamily	c.14.1 — ClpP/crotonase
Family Family family	c.14.1.1 — Clp protease, ClpP subunit

Domain ID domain_id	d3mt6g_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.14 — ClpP/crotonase
Superfamily Superfamily superfamily	c.14.1 — ClpP/crotonase
Family Family family	c.14.1.1 — Clp protease, ClpP subunit

Domain ID domain_id	d3mt6h_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.14 — ClpP/crotonase
Superfamily Superfamily superfamily	c.14.1 — ClpP/crotonase
Family Family family	c.14.1.1 — Clp protease, ClpP subunit

Domain ID domain_id	d3mt6i_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.14 — ClpP/crotonase
Superfamily Superfamily superfamily	c.14.1 — ClpP/crotonase
Family Family family	c.14.1.1 — Clp protease, ClpP subunit

Domain ID domain_id	d3mt6j_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.14 — ClpP/crotonase
Superfamily Superfamily superfamily	c.14.1 — ClpP/crotonase
Family Family family	c.14.1.1 — Clp protease, ClpP subunit

Domain ID domain_id	d3mt6k_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.14 — ClpP/crotonase
Superfamily Superfamily superfamily	c.14.1 — ClpP/crotonase
Family Family family	c.14.1.1 — Clp protease, ClpP subunit

Domain ID domain_id	d3mt6l_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.14 — ClpP/crotonase
Superfamily Superfamily superfamily	c.14.1 — ClpP/crotonase
Family Family family	c.14.1.1 — Clp protease, ClpP subunit

Domain ID domain_id	d3mt6m_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.14 — ClpP/crotonase
Superfamily Superfamily superfamily	c.14.1 — ClpP/crotonase
Family Family family	c.14.1.1 — Clp protease, ClpP subunit

Domain ID domain_id	d3mt6n_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.14 — ClpP/crotonase
Superfamily Superfamily superfamily	c.14.1 — ClpP/crotonase
Family Family family	c.14.1.1 — Clp protease, ClpP subunit

Domain ID domain_id	d3mt6o_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.14 — ClpP/crotonase
Superfamily Superfamily superfamily	c.14.1 — ClpP/crotonase
Family Family family	c.14.1.1 — Clp protease, ClpP subunit

Domain ID domain_id	d3mt6p_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.14 — ClpP/crotonase
Superfamily Superfamily superfamily	c.14.1 — ClpP/crotonase
Family Family family	c.14.1.1 — Clp protease, ClpP subunit

Domain ID domain_id	d3mt6q_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.14 — ClpP/crotonase
Superfamily Superfamily superfamily	c.14.1 — ClpP/crotonase
Family Family family	c.14.1.1 — Clp protease, ClpP subunit

Domain ID domain_id	d3mt6r_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.14 — ClpP/crotonase
Superfamily Superfamily superfamily	c.14.1 — ClpP/crotonase
Family Family family	c.14.1.1 — Clp protease, ClpP subunit

Domain ID domain_id	d3mt6s_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.14 — ClpP/crotonase
Superfamily Superfamily superfamily	c.14.1 — ClpP/crotonase
Family Family family	c.14.1.1 — Clp protease, ClpP subunit

Domain ID domain_id	d3mt6t_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.14 — ClpP/crotonase
Superfamily Superfamily superfamily	c.14.1 — ClpP/crotonase
Family Family family	c.14.1.1 — Clp protease, ClpP subunit

Domain ID domain_id	d3mt6u_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.14 — ClpP/crotonase
Superfamily Superfamily superfamily	c.14.1 — ClpP/crotonase
Family Family family	c.14.1.1 — Clp protease, ClpP subunit

Domain ID domain_id	d3mt6v_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.14 — ClpP/crotonase
Superfamily Superfamily superfamily	c.14.1 — ClpP/crotonase
Family Family family	c.14.1.1 — Clp protease, ClpP subunit

Domain ID domain_id	d3mt6w_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.14 — ClpP/crotonase
Superfamily Superfamily superfamily	c.14.1 — ClpP/crotonase
Family Family family	c.14.1.1 — Clp protease, ClpP subunit

Domain ID domain_id	d3mt6x_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.14 — ClpP/crotonase
Superfamily Superfamily superfamily	c.14.1 — ClpP/crotonase
Family Family family	c.14.1.1 — Clp protease, ClpP subunit

Domain ID domain_id	d3mt6y_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.14 — ClpP/crotonase
Superfamily Superfamily superfamily	c.14.1 — ClpP/crotonase
Family Family family	c.14.1.1 — Clp protease, ClpP subunit

Domain ID domain_id	d3mt6z_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.14 — ClpP/crotonase
Superfamily Superfamily superfamily	c.14.1 — ClpP/crotonase
Family Family family	c.14.1.1 — Clp protease, ClpP subunit

CATH v4.4 (28 domains)

Domain ID domain_id	3mt6A00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6B00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6C00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6D00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6E00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6F00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6G00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6H00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6I00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6J00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6K00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6L00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6M00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6N00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6O00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6P00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6Q00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6R00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6S00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6T00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6U00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6V00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6W00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6X00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6Y00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6Z00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6a00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

Domain ID domain_id	3mt6b00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	226 — 2-enoyl-CoA Hydratase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — 2-enoyl-CoA Hydratase; Chain A, domain 1

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8. Citations (1)

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Unit-cell length a length_a	93.254 Å
Unit-cell length b length_b	121.150 Å
Unit-cell length c length_c	276.170 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	91.38 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	56

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	1.901 Å
Low-resolution limit resolution_low	29.902 Å
R factor r_factor	0.1784
R_work r_work	0.1781
R_free r_free	0.2039

Structure of ClpP from Escherichia coli in complex with ADEP1

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

ATP-dependent Clp protease proteolytic subunit

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

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

7. Fold Classification (SCOP + CATH) 54 domains

SCOP 2.08 (26 domains)

CATH v4.4 (28 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/mt/3mt6/3mt6.fit
pddf	/app/data/pr_computation/mt/3mt6/3mt6.pr.out
profile	/app/data/saxs_computation/mt/3mt6/3mt6.dat