3o2h

E. coli ClpS in complex with a Leu N-end rule peptide

Method: X-RAY DIFFRACTION D_max: 53.7 Å Quality: REASONABLE

▼

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

ATP-dependent Clp protease adaptor protein ClpS

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 2–106	Not recorded	DNA protection during starvation protein × 1 （P0ABT2）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8.5；300 K；0.2 M Sodium Acetate, 0.1 M TRIS, 30% PEG 4000, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 300K	Resolution 1.70 Å R-free 0.224

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 3O2H	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1LZW Structural basis of ClpS-mediated switch in ClpA substrate recognition Deposited 2002-06-11	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–106（106 aa）	Mutation：H66A	PT PLATINUM (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；20% iPr, 20% PEG 4000, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 100K	Resolution 2.50 Å R-free 0.267
1LZW Structural basis of ClpS-mediated switch in ClpA substrate recognition Deposited 2002-06-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–106（106 aa）	Mutation：H66A	PT PLATINUM (II) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；20% iPr, 20% PEG 4000, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 100K	Resolution 2.50 Å R-free 0.267
1MBU Crystal Structure Analysis of ClpSN heterodimer Deposited 2002-08-03	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–106（106 aa）	Not recorded	YBT BIS-(2-HYDROXYETHYL)AMINO-TRIS(HYDROXYMETHYL)METHANE YTTRIUM × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å R-free 0.251
1MBU Crystal Structure Analysis of ClpSN heterodimer Deposited 2002-08-03	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–106（106 aa）	Not recorded	YBT BIS-(2-HYDROXYETHYL)AMINO-TRIS(HYDROXYMETHYL)METHANE YTTRIUM × 3 GOL GLYCEROL × 1 CL CHLORIDE ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å R-free 0.251
1MBV CRYSTAL STRUCTURE ANALYSIS OF ClpSN HETERODIMER TETRAGONAL FORM Deposited 2002-08-03	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–106（106 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.30 Å R-free 0.280
1MBX CRYSTAL STRUCTURE ANALYSIS OF ClpSN WITH TRANSITION METAL ION BOUND Deposited 2002-08-03	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–106（106 aa）	Not recorded	ZN ZINC ION × 1 YBT BIS-(2-HYDROXYETHYL)AMINO-TRIS(HYDROXYMETHYL)METHANE YTTRIUM × 2 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.7；294 K；glycerol, bis-tris , yttrium chloride, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 21K	Resolution 2.25 Å R-free 0.231
1MBX CRYSTAL STRUCTURE ANALYSIS OF ClpSN WITH TRANSITION METAL ION BOUND Deposited 2002-08-03	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–106（106 aa）	Not recorded	ZN ZINC ION × 1 YBT BIS-(2-HYDROXYETHYL)AMINO-TRIS(HYDROXYMETHYL)METHANE YTTRIUM × 3 GOL GLYCEROL × 2 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.7；294 K；glycerol, bis-tris , yttrium chloride, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 21K	Resolution 2.25 Å R-free 0.231
1MG9 The structural basis of ClpS-mediated switch in ClpA substrate recognition Deposited 2002-08-15	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–106（106 aa）	Mutation：H66A	SPK SPERMINE (FULLY PROTONATED FORM) × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；i-PR, PEG8000, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 18K	Resolution 2.30 Å R-free 0.294
1R6O ATP-dependent Clp protease ATP-binding subunit clpA/ATP-dependent Clp protease adaptor protein clpS Deposited 2003-10-15	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–106（106 aa）	Not recorded	ZN ZINC ION × 1 YBT BIS-(2-HYDROXYETHYL)AMINO-TRIS(HYDROXYMETHYL)METHANE YTTRIUM × 2 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions 294 K；Drop: 0.02M Tris HCl (pH 8.5), 2mM ZnCl2, 10% (w/v) glycerol; Precipitant: 0.1M bis-tris (pH 6.5), 32% (w/v) glycerol, 0.01-0.015M yttrium chloride, HANGING DROP, temperature 294K	Resolution 2.25 Å R-free 0.205
1R6O ATP-dependent Clp protease ATP-binding subunit clpA/ATP-dependent Clp protease adaptor protein clpS Deposited 2003-10-15	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–106（106 aa）	Not recorded	ZN ZINC ION × 1 YBT BIS-(2-HYDROXYETHYL)AMINO-TRIS(HYDROXYMETHYL)METHANE YTTRIUM × 2 GOL GLYCEROL × 2 CL CHLORIDE ION × 1 Y1 YTTRIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions 294 K；Drop: 0.02M Tris HCl (pH 8.5), 2mM ZnCl2, 10% (w/v) glycerol; Precipitant: 0.1M bis-tris (pH 6.5), 32% (w/v) glycerol, 0.01-0.015M yttrium chloride, HANGING DROP, temperature 294K	Resolution 2.25 Å R-free 0.205
1R6O ATP-dependent Clp protease ATP-binding subunit clpA/ATP-dependent Clp protease adaptor protein clpS Deposited 2003-10-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–106（106 aa） Chain D 1–106（106 aa）	Not recorded	ZN ZINC ION × 2 YBT BIS-(2-HYDROXYETHYL)AMINO-TRIS(HYDROXYMETHYL)METHANE YTTRIUM × 4 GOL GLYCEROL × 3 CL CHLORIDE ION × 1 Y1 YTTRIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions 294 K；Drop: 0.02M Tris HCl (pH 8.5), 2mM ZnCl2, 10% (w/v) glycerol; Precipitant: 0.1M bis-tris (pH 6.5), 32% (w/v) glycerol, 0.01-0.015M yttrium chloride, HANGING DROP, temperature 294K	Resolution 2.25 Å R-free 0.205
1R6Q ClpNS with fragments Deposited 2003-10-16	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–106（106 aa）	Not recorded	YBT BIS-(2-HYDROXYETHYL)AMINO-TRIS(HYDROXYMETHYL)METHANE YTTRIUM × 2 GOL GLYCEROL × 1 Y1 YTTRIUM ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.35 Å R-free 0.223
1R6Q ClpNS with fragments Deposited 2003-10-16	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–106（106 aa）	Not recorded	YBT BIS-(2-HYDROXYETHYL)AMINO-TRIS(HYDROXYMETHYL)METHANE YTTRIUM × 2 GOL GLYCEROL × 1 Y1 YTTRIUM ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.35 Å R-free 0.223
1R6Q ClpNS with fragments Deposited 2003-10-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–106（106 aa） Chain D 1–106（106 aa）	Not recorded	YBT BIS-(2-HYDROXYETHYL)AMINO-TRIS(HYDROXYMETHYL)METHANE YTTRIUM × 4 GOL GLYCEROL × 2 Y1 YTTRIUM ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.35 Å R-free 0.223
2W9R Structural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP adaptor protein ClpS Deposited 2009-01-28	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–106（106 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；pH 7	Resolution 1.70 Å R-free 0.254
2WA8 Structural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP adaptor protein ClpS - The Phe peptide structure Deposited 2009-02-03	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–106（106 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；pH 8.5	Resolution 2.15 Å R-free 0.268
2WA8 Structural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP adaptor protein ClpS - The Phe peptide structure Deposited 2009-02-03	Different construct Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–106（106 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；pH 8.5	Resolution 2.15 Å R-free 0.268
2WA9 Structural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP adaptor protein ClpS - Trp peptide structure Deposited 2009-02-03	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–106（106 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；pH 8.5	Resolution 2.90 Å R-free 0.248
2WA9 Structural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP adaptor protein ClpS - Trp peptide structure Deposited 2009-02-03	Different construct Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–106（106 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；pH 8.5	Resolution 2.90 Å R-free 0.248
2WA9 Structural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP adaptor protein ClpS - Trp peptide structure Deposited 2009-02-03	Different construct Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–106（106 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；pH 8.5	Resolution 2.90 Å R-free 0.248
2WA9 Structural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP adaptor protein ClpS - Trp peptide structure Deposited 2009-02-03	Different construct Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–106（106 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；pH 8.5	Resolution 2.90 Å R-free 0.248
2WA9 Structural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP adaptor protein ClpS - Trp peptide structure Deposited 2009-02-03	Different construct Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 1–106（106 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；pH 8.5	Resolution 2.90 Å R-free 0.248
2WA9 Structural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP adaptor protein ClpS - Trp peptide structure Deposited 2009-02-03	Different construct Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 1–106（106 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；pH 8.5	Resolution 2.90 Å R-free 0.248
2WA9 Structural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP adaptor protein ClpS - Trp peptide structure Deposited 2009-02-03	Different construct Different experimental conditions Different structure-quality metrics	Assembly 7 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain G 1–106（106 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；pH 8.5	Resolution 2.90 Å R-free 0.248
3O2B E. coli ClpS in complex with a Phe N-end rule peptide Deposited 2010-07-22	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 2–106（105 aa） Fragment：unp residues 2-106	Not recorded	SO4 SULFATE ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；300 K；2 M Lithium Sulfate, 0.1 M TRIS, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 300K	Resolution 2.05 Å R-free 0.247
3O2B E. coli ClpS in complex with a Phe N-end rule peptide Deposited 2010-07-22	Different construct Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 2–106（105 aa） Fragment：unp residues 2-106	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；300 K；2 M Lithium Sulfate, 0.1 M TRIS, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 300K	Resolution 2.05 Å R-free 0.247
3O2O Structure of E. coli ClpS ring complex Deposited 2010-07-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 22–106（85 aa） Fragment：unp residues 22-106 Chain B 22–106（85 aa） Fragment：unp residues 22-106	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；300 K；0.1 M Sodium Nitrate 20% PEG 3350, pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 300K	Resolution 2.90 Å R-free 0.201
3O2O Structure of E. coli ClpS ring complex Deposited 2010-07-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 22–106（85 aa） Fragment：unp residues 22-106 Chain C 22–106（85 aa） Fragment：unp residues 22-106	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；300 K；0.1 M Sodium Nitrate 20% PEG 3350, pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 300K	Resolution 2.90 Å R-free 0.201
3O2O Structure of E. coli ClpS ring complex Deposited 2010-07-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 22–106（85 aa） Fragment：unp residues 22-106 Chain D 22–106（85 aa） Fragment：unp residues 22-106	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；300 K；0.1 M Sodium Nitrate 20% PEG 3350, pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 300K	Resolution 2.90 Å R-free 0.201
3O2O Structure of E. coli ClpS ring complex Deposited 2010-07-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain D 22–106（85 aa） Fragment：unp residues 22-106 Chain E 22–106（85 aa） Fragment：unp residues 22-106	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；300 K；0.1 M Sodium Nitrate 20% PEG 3350, pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 300K	Resolution 2.90 Å R-free 0.201
3O2O Structure of E. coli ClpS ring complex Deposited 2010-07-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain E 22–106（85 aa） Fragment：unp residues 22-106 Chain F 22–106（85 aa） Fragment：unp residues 22-106	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；300 K；0.1 M Sodium Nitrate 20% PEG 3350, pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 300K	Resolution 2.90 Å R-free 0.201
3O2O Structure of E. coli ClpS ring complex Deposited 2010-07-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 6 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain F 22–106（85 aa） Fragment：unp residues 22-106 Chain G 22–106（85 aa） Fragment：unp residues 22-106	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；300 K；0.1 M Sodium Nitrate 20% PEG 3350, pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 300K	Resolution 2.90 Å R-free 0.201
3O2O Structure of E. coli ClpS ring complex Deposited 2010-07-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 7 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain G 22–106（85 aa） Fragment：unp residues 22-106 Chain H 22–106（85 aa） Fragment：unp residues 22-106	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；300 K；0.1 M Sodium Nitrate 20% PEG 3350, pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 300K	Resolution 2.90 Å R-free 0.201
3O2O Structure of E. coli ClpS ring complex Deposited 2010-07-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 8 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 22–106（85 aa） Fragment：unp residues 22-106 Chain H 22–106（85 aa） Fragment：unp residues 22-106	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；300 K；0.1 M Sodium Nitrate 20% PEG 3350, pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 300K	Resolution 2.90 Å R-free 0.201

12 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CLPS_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–105； UniProt 2–106

DNA protection during starvation protein

OrganismNot specified

UniProt P0ABT2

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 6–16	Fragment：unp residues 6-16	ATP-dependent Clp protease adaptor protein ClpS × 1 （P0A8Q6）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8.5；300 K；0.2 M Sodium Acetate, 0.1 M TRIS, 30% PEG 4000, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 300K	Resolution 1.70 Å R-free 0.224

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 3O2H	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1DPS THE CRYSTAL STRUCTURE OF DPS, A FERRITIN HOMOLOG THAT BINDS AND PROTECTS DNA Deposited 1998-02-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 1–166（166 aa） Chain B 1–166（166 aa） Chain C 1–166（166 aa） Chain D 1–166（166 aa） Chain E 1–166（166 aa） Chain F 1–166（166 aa） Chain G 1–166（166 aa） Chain H 1–166（166 aa） Chain I 1–166（166 aa） Chain J 1–166（166 aa） Chain K 1–166（166 aa） Chain L 1–166（166 aa）	Mutation：S164C Mutation：S164C Mutation：S164C Mutation：S164C Mutation：S164C Mutation：S164C Mutation：S164C Mutation：S164C Mutation：S164C Mutation：S164C Mutation：S164C Mutation：S164C	NA SODIUM ION × 12	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；1.55-1.7 M SODIUM FORMATE 13-16% PEG 8000 100 MM NACL 50 MM TRIS PH 8, pH 8.0	Resolution 1.60 Å R-free 0.220
1F30 THE STRUCTURAL BASIS FOR DNA PROTECTION BY E. COLI DPS PROTEIN Deposited 2000-05-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 0–166（167 aa） Chain B 0–166（167 aa） Chain C 0–166（167 aa） Chain D 0–166（167 aa） Chain E 0–166（167 aa） Chain F 0–166（167 aa）	Not recorded	ZN ZINC ION × 12 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.1；298 K；10mM MOPS, 100mM KCl, 10% glycerol + 100mM TrisHCL, 100mM KCl, 10% glycerol, 11% PEG 8000, and 5mM DTT, pH 8.1, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.85 Å R-free 0.272
1F30 THE STRUCTURAL BASIS FOR DNA PROTECTION BY E. COLI DPS PROTEIN Deposited 2000-05-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain G 0–166（167 aa） Chain H 0–166（167 aa） Chain I 0–166（167 aa） Chain J 0–166（167 aa） Chain K 0–166（167 aa） Chain L 0–166（167 aa）	Not recorded	ZN ZINC ION × 12 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.1；298 K；10mM MOPS, 100mM KCl, 10% glycerol + 100mM TrisHCL, 100mM KCl, 10% glycerol, 11% PEG 8000, and 5mM DTT, pH 8.1, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.85 Å R-free 0.272
1F33 THE STRUCTURAL BASIS FOR DNA PROTECTION BY E. COLI DPS PROTEIN Deposited 2000-05-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 0–166（167 aa） Chain B 0–166（167 aa） Chain C 0–166（167 aa） Chain D 0–166（167 aa） Chain E 0–166（167 aa） Chain F 0–166（167 aa）	Not recorded	TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.1；298 K；10mM MOPS, 100mM KCl, 10% glycerol + 100mM TrisHCL, 100mM KCl, 10% glycerol, 11% PEG 8000, and 5mM DTT , pH 8.1, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.60 Å R-free 0.244
1F33 THE STRUCTURAL BASIS FOR DNA PROTECTION BY E. COLI DPS PROTEIN Deposited 2000-05-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain G 0–166（167 aa） Chain H 0–166（167 aa） Chain I 0–166（167 aa） Chain J 0–166（167 aa） Chain K 0–166（167 aa） Chain L 0–166（167 aa）	Not recorded	TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.1；298 K；10mM MOPS, 100mM KCl, 10% glycerol + 100mM TrisHCL, 100mM KCl, 10% glycerol, 11% PEG 8000, and 5mM DTT , pH 8.1, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.60 Å R-free 0.244
1F33 THE STRUCTURAL BASIS FOR DNA PROTECTION BY E. COLI DPS PROTEIN Deposited 2000-05-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 0–166（167 aa） Chain B 0–166（167 aa） Chain C 0–166（167 aa） Chain D 0–166（167 aa） Chain E 0–166（167 aa） Chain F 0–166（167 aa）	Not recorded	TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.1；298 K；10mM MOPS, 100mM KCl, 10% glycerol + 100mM TrisHCL, 100mM KCl, 10% glycerol, 11% PEG 8000, and 5mM DTT , pH 8.1, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.60 Å R-free 0.244
1JRE DNA PROTECTION AND BINDING BY E. COLI DPS PROTEIN Deposited 2001-08-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 0–166（167 aa） Chain B 0–166（167 aa） Chain C 0–166（167 aa） Chain D 0–166（167 aa） Chain E 0–166（167 aa） Chain F 0–166（167 aa） Chain G 0–166（167 aa） Chain H 0–166（167 aa） Chain I 0–166（167 aa） Chain J 0–166（167 aa） Chain K 0–166（167 aa） Chain L 0–166（167 aa）	Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A	CD CADMIUM ION × 13 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.1；298 K；10MM MOPS, 100MM KCL, 10% GLYCEROL + 100MM TRISHCL, 100MM KCL, 10% GLYCEROL, 11% PEG 8000, AND 5MM DTT, pH 8.10, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.65 Å R-free 0.264
1JTS DNA PROTECTION AND BINDING BY E. COLI DPS PROTEIN Deposited 2001-08-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 0–166（167 aa） Chain B 0–166（167 aa） Chain C 0–166（167 aa） Chain D 0–166（167 aa） Chain E 0–166（167 aa） Chain F 0–166（167 aa） Chain G 0–166（167 aa） Chain H 0–166（167 aa） Chain I 0–166（167 aa） Chain J 0–166（167 aa） Chain K 0–166（167 aa） Chain L 0–166（167 aa）	Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A	TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.1；298 K；10MM MOPS, 100MM KCL, 10% GLYCEROL + 100MM TRISHCL, 100MM KCL, 10% GLYCEROL, 11% PEG 8000, AND 5MM DTT, pH 8.10, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 2.60 Å R-free 0.268
1JTS DNA PROTECTION AND BINDING BY E. COLI DPS PROTEIN Deposited 2001-08-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain M 0–166（167 aa） Chain N 0–166（167 aa） Chain O 0–166（167 aa） Chain P 0–166（167 aa） Chain Q 0–166（167 aa） Chain R 0–166（167 aa） Chain S 0–166（167 aa） Chain T 0–166（167 aa） Chain U 0–166（167 aa） Chain V 0–166（167 aa） Chain W 0–166（167 aa） Chain X 0–166（167 aa）	Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A	TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.1；298 K；10MM MOPS, 100MM KCL, 10% GLYCEROL + 100MM TRISHCL, 100MM KCL, 10% GLYCEROL, 11% PEG 8000, AND 5MM DTT, pH 8.10, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 2.60 Å R-free 0.268
1L8H DNA PROTECTION AND BINDING BY E. COLI DPS PROTEIN Deposited 2002-03-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 0–166（167 aa） Chain B 0–166（167 aa） Chain C 0–166（167 aa） Chain D 0–166（167 aa） Chain E 0–166（167 aa） Chain F 0–166（167 aa） Chain G 0–166（167 aa） Chain H 0–166（167 aa） Chain I 0–166（167 aa） Chain J 0–166（167 aa） Chain K 0–166（167 aa） Chain L 0–166（167 aa）	Mutation：D75C/D78A Mutation：D75C/D78A Mutation：D75C/D78A Mutation：D75C/D78A Mutation：D75C/D78A Mutation：D75C/D78A Mutation：D75C/D78A Mutation：D75C/D78A Mutation：D75C/D78A Mutation：D75C/D78A Mutation：D75C/D78A Mutation：D75C/D78A	K POTASSIUM ION × 12 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.1；298 K；10MM MOPS, 100MM KCL, 10%GLYCEROL + 100MM TRISHCL, 100MM KCL, 10% GLYCEROL, 11% PEG 8000, AND 5MM DTT, pH 8.10, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.20 Å R-free 0.250
1L8I Dna Protection and Binding by E. Coli DPS Protein Deposited 2002-03-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 0–166（167 aa） Chain B 0–166（167 aa） Chain C 0–166（167 aa） Chain D 0–166（167 aa） Chain E 0–166（167 aa） Chain F 0–166（167 aa） Chain G 0–166（167 aa） Chain H 0–166（167 aa） Chain I 0–166（167 aa） Chain J 0–166（167 aa） Chain K 0–166（167 aa） Chain L 0–166（167 aa）	Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A Mutation：D75C, D78A	K POTASSIUM ION × 12 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.1；298 K；10MM MOPS, 100MM KCL, 10%GLYCEROL + 100MM TRISHCL, 100MM KCL, 10% GLYCEROL, 11% PEG 8000, AND 5MM DTT, pH 8.10, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.00 Å R-free 0.250
2W9R Structural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP adaptor protein ClpS Deposited 2009-01-28	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 6–16（11 aa） Fragment：RESIDUES 10-16	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；pH 7	Resolution 1.70 Å R-free 0.254
5XGO The Ferritin E-Domain: Toward Understanding Its Role in Protein Cage Assembly Through the Crystal Structure of a Maxi-/Mini-Ferritin Chimera Deposited 2017-04-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 1–163（163 aa） Chain B 1–163（163 aa） Chain C 1–163（163 aa） Chain D 1–163（163 aa） Chain E 1–163（163 aa） Chain F 1–163（163 aa） Chain G 1–163（163 aa） Chain H 1–163（163 aa） Chain I 1–163（163 aa） Chain J 1–163（163 aa） Chain K 1–163（163 aa） Chain L 1–163（163 aa）	Not recorded	CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 4.2；292.15 K；0.2M lithium sulphate, 18% PEG 1000, pH 4.2	Resolution 1.99 Å R-free 0.207
6GCM Escherichia coli DPS Deposited 2018-04-18	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 9–167（159 aa） Chain B 14–167（154 aa） Chain C 14–167（154 aa） Chain D 12–167（156 aa） Chain E 14–167（154 aa） Chain F 14–167（154 aa） Chain G 14–167（154 aa） Chain H 14–167（154 aa） Chain I 14–167（154 aa） Chain J 14–167（154 aa） Chain K 14–167（154 aa） Chain L 14–167（154 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION, RECRYSTALLIZATION；291 K；PEG 8000	Resolution 2.45 Å R-free 0.258
6GCM Escherichia coli DPS Deposited 2018-04-18	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain b 9–167（159 aa） Chain c 14–167（154 aa） Chain d 14–167（154 aa） Chain e 12–167（156 aa） Chain f 17–167（151 aa） Chain g 14–167（154 aa） Chain h 14–167（154 aa） Chain i 14–167（154 aa） Chain j 14–167（154 aa） Chain k 14–167（154 aa） Chain l 14–167（154 aa） Chain m 14–167（154 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION, RECRYSTALLIZATION；291 K；PEG 8000	Resolution 2.45 Å R-free 0.258
7AQS Crystal structure of E. coli DPS in space group P1 Deposited 2020-10-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 1–167（167 aa） Chain B 1–167（167 aa） Chain C 1–167（167 aa） Chain D 1–167（167 aa） Chain E 1–167（167 aa） Chain F 1–167（167 aa） Chain G 1–167（167 aa） Chain H 1–167（167 aa） Chain I 1–167（167 aa） Chain J 1–167（167 aa） Chain K 1–167（167 aa） Chain L 1–167（167 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	FE FE (III) ION × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1 M HEPES pH 7.0, 6.73 % w/v PEG 5000 MME and 0.06 M KCl	Resolution 2.80 Å R-free 0.243
7AQS Crystal structure of E. coli DPS in space group P1 Deposited 2020-10-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain M 1–167（167 aa） Chain N 1–167（167 aa） Chain O 1–167（167 aa） Chain P 1–167（167 aa） Chain Q 1–167（167 aa） Chain R 1–167（167 aa） Chain S 1–167（167 aa） Chain T 1–167（167 aa） Chain U 1–167（167 aa） Chain V 1–167（167 aa） Chain W 1–167（167 aa） Chain X 1–167（167 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	FE FE (III) ION × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1 M HEPES pH 7.0, 6.73 % w/v PEG 5000 MME and 0.06 M KCl	Resolution 2.80 Å R-free 0.243
8OUC Escherichia coli DPS Deposited 2023-04-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain AAA 1–167（167 aa） Chain BBB 1–167（167 aa） Chain CCC 1–167（167 aa） Chain DDD 1–167（167 aa） Chain EEE 1–167（167 aa） Chain FFF 1–167（167 aa） Chain GGG 1–167（167 aa） Chain HHH 1–167（167 aa） Chain III 1–167（167 aa） Chain JJJ 1–167（167 aa） Chain KKK 1–167（167 aa） Chain LLL 1–167（167 aa）	Not recorded	TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 7	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.3；290 K；TRIS-HCl	Resolution 1.37 Å R-free 0.206
8PV9 Structure of DPS determined by cryoEM at 100 keV Deposited 2023-07-17	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: 12-meric	Chain A 2–167（166 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.70 Å
9ZC2 Structure of E. Coli DNA protection during starvation protein (DPS) from single particle cryoEM Deposited 2025-11-22	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 × 12 PDB declaration: 12-meric	Chain A 1–167（167 aa） Chain B 1–167（167 aa） Chain C 1–167（167 aa） Chain D 1–167（167 aa） Chain E 1–167（167 aa） Chain F 1–167（167 aa） Chain G 1–167（167 aa） Chain H 1–167（167 aa） Chain I 1–167（167 aa） Chain J 1–167（167 aa） Chain K 1–167（167 aa） Chain L 1–167（167 aa）	Not recorded	FE FE (III) ION × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 1.30 Å

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

View Construct and Data Evidence

UniProt name	DPS_ECOLI
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–11； UniProt 6–16

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

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	3o2h
Deposition date deposition_date	2010-07-22
Structure title title	E. coli ClpS in complex with a Leu N-end rule peptide
Keywords keywords	adaptor, protein-peptide complex, peptide-binding protein, N-end rule peptide, PEPTIDE BINDING PROTEIN; PEPTIDE BINDING PROTEIN
Experimental Method method	X-RAY DIFFRACTION

▼

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

Radius of gyration Rg (Guinier) rg_guinier	19.04 Å
Radius of gyration Rg (electron density) rg_electron	19.16 Å
Forward intensity I(0) i0	2686010.00
Molecular weight molecular_weight	12017.0 kDa
Excluded volume excluded_volume	15305 Å³
Envelope volume envelope_volume	19693 Å³
Hydration-shell volume shell_volume	10620 Å³
Envelope diameter envelope_diameter	88.8 Å
Shell Rg shell_rg	22.03 Å
Envelope Rg envelope_rg	21.46 Å
Shape Rg shape_rg	19.15 Å
Total Rg total_rg	19.77 Å
Total atoms total_atoms	1701
Residues n_residues	106
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

▼

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

Maximum dimension Dmax dmax	53.7 Å
Rg (real space) rg_real	17.60 Å
Rg uncertainty (real space) rg_real_error	0.13 Å
I(0) (real space) i0_real	2.5660e+06
I(0) uncertainty (real space) i0_real_error	2.2950e+04
Rg (reciprocal space) rg_reciprocal	19.61 Å
I(0) (reciprocal space) i0_reciprocal	2686000.0000
Solution quality estimate total_estimate	0.6395
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	18.6 Å
Skewness Skewness skewness	0.650
Kurtosis Kurtosis kurtosis	-0.086
Angular range angular_range	— – 0.4200 Å⁻¹
Current regularization parameter α current_alpha	2.4740
Highest regularization parameter α highest_alpha	246200.0000
Real-space data points n_real_points	73
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.013; Oscil: 0.832; Stabil: 0.981; Sysdev: 0.000; Positv: 1.000; Valcen: 0.886; Smooth: 0.000

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	ATP-dependent Clp protease adaptor protein ClpS
Molecular weight formula_weight	12061.8 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1833

GKTNDWLDFDQLAEEKVRDALKPPSMYKVILVNDDYTPMEFVIDVLQKFFSYDVERATQLMLAVHYQGKAICGVFTAEVAETKVAMVNKYARENEHPLLCTLEKA

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	DNA protection during starvation protein
Molecular weight formula_weight	1251.5 kDa
EC 编号 ec_number	1.16.-.-
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

LVKSKATNLLY

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	121

▼

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d3o2ha_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.45 — ClpS-like
Superfamily Superfamily superfamily	d.45.1 — ClpS-like
Family Family family	d.45.1.2 — Adaptor protein ClpS (YljA)

CATH v4.4 (1 domains)

Domain ID domain_id	3o2hA01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1390 — Ribosomal Protein L30; Chain: A,
Homologous superfamily homologous superfamily	10 — Ribosomal protein L7/L12, C-terminal domain/Adaptor protein ClpS

▶

8. Citations (2)

▶

Unit-cell length a length_a	28.080 Å
Unit-cell length b length_b	28.230 Å
Unit-cell length c length_c	38.910 Å
Unit-cell angle α angle_alpha	97.44 °
Unit-cell angle β angle_beta	106.45 °
Unit-cell angle γ angle_gamma	92.39 °
Molecules per unit cell Z z_pdb	1

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

Resolution resolution	1.700 Å
Low-resolution limit resolution_low	18.455 Å
R factor r_factor	0.2002
R_work r_work	0.1989
R_free r_free	0.2242

fit	/app/data/saxs_computation/o2/3o2h/3o2h.fit
pddf	/app/data/pr_computation/o2/3o2h/3o2h.pr.out
profile	/app/data/saxs_computation/o2/3o2h/3o2h.dat

E. coli ClpS in complex with a Leu N-end rule peptide

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

ATP-dependent Clp protease adaptor protein ClpS

State in the Current Structure

Other States of the Same Protein in the Database

DNA protection during starvation protein

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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)