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3k0s

Crystal structure of E.coli DNA mismatch repair protein MutS, D693N mutant, in complex with GT mismatched DNA

Method: X-RAY DIFFRACTION Dmax: 131.0 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

DNA mismatch repair protein mutS

Escherichia coli

UniProt P23909

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–DNA Homooligomer Protein × 2 DNA 2 PDB declaration: tetrameric（4） Consistent with all polymer counts Chain A； UniProt 2–800 Chain B； UniProt 2–800 Fragment：UNP residues 2-800 Mutation：D693N 5'-D(*AP*GP*CP*TP*GP*CP*CP*AP*GP*GP*CP*AP*CP*CP*AP*GP*TP*GP*TP*CP*AP*GP*CP*GP*TP*CP*CP*TP*AP*T)-3' × 1 5'-D(*AP*TP*AP*GP*GP*AP*CP*GP*CP*TP*GP*AP*C*AP*CP*T*GP*GP*TP*GP*CP*TP*TP*GP*GP*CP*AP*GP*CP*T)-3' × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；11% PEG 6000, 750mM NaCl, 25mM Hepes, 10mM MgCl2, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.20 Å R-free 0.246

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 3K0S Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1E3M The crystal structure of E. coli MutS binding to DNA with a G:T mismatch Deposited 2000-06-19 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 1–800（800 aa） Fragment：RESIDUES 1-800
Chain B 1–800（800 aa） Fragment：RESIDUES 1-800
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；12-14 % PEG 6000, 150-300 MM NACL, 100 MM HEPES PH 7-8, 10 MM MGCL2, 100-150 MICROM ADP
Resolution 2.20 Å R-free 0.266
1NG9 E.coli MutS R697A: an ATPase-asymmetry mutant Deposited 2002-12-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 1–800（800 aa） Fragment：residues 1-800
Chain B 1–800（800 aa） Fragment：residues 1-800
Mutation：R697A Mutation：R697A MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；297 K；PEG 6000, NaCl, MgCl2, HEPES, ADP, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 297K
Resolution 2.60 Å R-free 0.249
1OH5 THE CRYSTAL STRUCTURE OF E. COLI MUTS BINDING TO DNA WITH A C:A MISMATCH Deposited 2003-05-23 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 1–800（800 aa） Fragment：RESIDUES 1-800
Chain B 1–800（800 aa） Fragment：RESIDUES 1-800
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；12-14 % PEG 6000, 150-300 MM NACL 25 MM HEPES PH 7-8, 10 MM MGCL2, 100-150 MICROM ADP
Resolution 2.90 Å R-free 0.294
1OH6 THE CRYSTAL STRUCTURE OF E. COLI MUTS BINDING TO DNA WITH AN A:A MISMATCH Deposited 2003-05-23 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 1–800（800 aa） Fragment：RESIDUES 1-800
Chain B 1–800（800 aa） Fragment：RESIDUES 1-800
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；12-14 % PEG 6000, 150-300 MM NACL 25 MM HEPES PH 7-8, 10 MM MGCL2, 100-150 MICROM ADP
Resolution 2.40 Å R-free 0.253
1OH7 THE CRYSTAL STRUCTURE OF E. COLI MUTS BINDING TO DNA WITH A G:G MISMATCH Deposited 2003-05-23 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 1–800（800 aa） Fragment：RESIDUES 1-800
Chain B 1–800（800 aa） Fragment：RESIDUES 1-800
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；12-14 % PEG 6000, 150-300 MM NACL 25 MM HEPES PH 7-8, 10 MM MGCL2, 100-150 MICROM ADP
Resolution 2.50 Å R-free 0.276
1OH8 THE CRYSTAL STRUCTURE OF E. COLI MUTS BINDING TO DNA WITH AN UNPAIRED THYMIDINE Deposited 2003-05-23 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 1–800（800 aa） Fragment：RESIDUES 1-800
Chain B 1–800（800 aa） Fragment：RESIDUES 1-800
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；12-14 % PEG 6000, 150-300 MM NACL 25 MM HEPES PH 7-8, 10 MM MGCL2, 100-150 MICROM ADP
Resolution 2.90 Å R-free 0.292
1W7A ATP bound MutS Deposited 2004-08-31 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 1–800（800 aa） Fragment：RESIDUES 1-800
Chain B 1–800（800 aa） Fragment：RESIDUES 1-800
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；12-14% PEG6000, 150-300MM NACL, 10 MM MGCL2, 25 MM HEPES PH 7.5, 100 UM ADP
Resolution 2.27 Å R-free 0.253
1WB9 Crystal Structure of E. coli DNA Mismatch Repair enzyme MutS, E38T mutant, in complex with a G.T mismatch Deposited 2004-10-31 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 1–800（800 aa） Fragment：RESIDUES 1-800
Chain B 1–800（800 aa） Fragment：RESIDUES 1-800
Mutation：YES Mutation：YES ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；25 MM HEPES(7.5), 300 MM NACL, 10 MM MGCL2, 14 % PEG 6000., pH 7.50
Resolution 2.10 Å R-free 0.234
1WBB Crystal structure of E. coli DNA mismatch repair enzyme MutS, E38A mutant, in complex with a G.T mismatch Deposited 2004-10-31 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 1–800（800 aa） Fragment：RESIDUES 1-800
Chain B 1–800（800 aa） Fragment：RESIDUES 1-800
Mutation：YES Mutation：YES ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；25 MM HEPES(7.5), 300 MM NACL, 10 MM MGCL2, 14 % PEG 6000., pH 7.50
Resolution 2.50 Å R-free 0.270
1WBD Crystal structure of E. coli DNA mismatch repair enzyme MutS, E38Q mutant, in complex with a G.T mismatch Deposited 2004-10-31 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 1–800（800 aa） Fragment：RESIDUES 1-800
Chain B 1–800（800 aa） Fragment：RESIDUES 1-800
Mutation：YES Mutation：YES ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；25 MM HEPES(7.5), 300 MM NACL, 10 MM MGCL2, 14 % PEG 6000., pH 7.50
Resolution 2.40 Å R-free 0.259
2OK2 MutS C-terminal domain fused to Maltose Binding Protein Deposited 2007-01-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 820–853（34 aa） Fragment：MBP/MutS C-terminal fusion
Chain B 820–853（34 aa） Fragment：MBP/MutS C-terminal fusion
Not recorded SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；298 K；15% PEG 4K, 100 mM sodium citrate, 100 mM lithium acetate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.00 Å R-free 0.277
2WTU Crystal structure of Escherichia coli MutS in complex with a 16 basepair oligo containing an A.A mismatch. Deposited 2009-09-22 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 1–800（800 aa） Fragment：RESIDUES 1-800
Chain B 1–800（800 aa） Fragment：RESIDUES 1-800
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 1 CL CHLORIDE ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；18% PEG 3350, 100 MM SODIUM CITRATE, 100 MM BIS TRIS PROPANE PH 7.5, 5 MM MGCL2, 100 MICROM ADP.
Resolution 3.40 Å R-free 0.263
3ZLJ CRYSTAL STRUCTURE OF FULL-LENGTH E.COLI DNA MISMATCH REPAIR PROTEIN MUTS D835R MUTANT IN COMPLEX WITH GT MISMATCHED DNA Deposited 2013-02-01 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 1–800（800 aa）
Chain B 1–800（800 aa）
Mutation：YES Mutation：YES No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；5MM TRIS PH8, 750MM NACL, 12% PEG 6000, 10MM MGCL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K, pH 7.5
Resolution 3.10 Å R-free 0.263
3ZLJ CRYSTAL STRUCTURE OF FULL-LENGTH E.COLI DNA MISMATCH REPAIR PROTEIN MUTS D835R MUTANT IN COMPLEX WITH GT MISMATCHED DNA Deposited 2013-02-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 801–853（53 aa）
Chain D 801–853（53 aa）
Mutation：YES Mutation：YES No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；5MM TRIS PH8, 750MM NACL, 12% PEG 6000, 10MM MGCL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K, pH 7.5
Resolution 3.10 Å R-free 0.263
5AKB MutS in complex with the N-terminal domain of MutL - crystal form 1 Deposited 2015-03-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–800（800 aa）
Chain B 1–800（800 aa）
Mutation：YES Mutation：YES ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions 9-12% PEG8000, 100 MM TRIS PH 7.0, 200 MM MGCL2, 80-450 MM SODIUM MALONATE
Resolution 4.71 Å R-free 0.349
5AKB MutS in complex with the N-terminal domain of MutL - crystal form 1 Deposited 2015-03-03 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 E 1–800（800 aa）
Mutation：YES ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions 9-12% PEG8000, 100 MM TRIS PH 7.0, 200 MM MGCL2, 80-450 MM SODIUM MALONATE
Resolution 4.71 Å R-free 0.349
5AKC MutS in complex with the N-terminal domain of MutL - crystal form 2 Deposited 2015-03-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–800（800 aa）
Chain B 1–800（800 aa）
Mutation：YES Mutation：YES ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions 9-12% PEG8000, 100 MM TRIS PH 7.0, 200 MM MGCL2, 80-450 MM SODIUM MALONATE
Resolution 6.60 Å R-free 0.291
5AKC MutS in complex with the N-terminal domain of MutL - crystal form 2 Deposited 2015-03-03 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 E 1–800（800 aa）
Chain F 1–800（800 aa）
Mutation：YES Mutation：YES ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions 9-12% PEG8000, 100 MM TRIS PH 7.0, 200 MM MGCL2, 80-450 MM SODIUM MALONATE
Resolution 6.60 Å R-free 0.291
5AKC MutS in complex with the N-terminal domain of MutL - crystal form 2 Deposited 2015-03-03 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 I 1–800（800 aa）
Chain J 1–800（800 aa）
Mutation：YES Mutation：YES ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions 9-12% PEG8000, 100 MM TRIS PH 7.0, 200 MM MGCL2, 80-450 MM SODIUM MALONATE
Resolution 6.60 Å R-free 0.291
5AKD MutS in complex with the N-terminal domain of MutL - crystal form 3 Deposited 2015-03-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–800（800 aa）
Chain B 1–800（800 aa）
Mutation：YES Mutation：YES ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions 9-12% PEG8000, 100 MM TRIS PH 7.0, 200 MM MGCL2, 80-450 MM SODIUM MALONATE
Resolution 7.60 Å R-free 0.306
5AKD MutS in complex with the N-terminal domain of MutL - crystal form 3 Deposited 2015-03-03 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 E 1–800（800 aa）
Chain F 1–800（800 aa）
Mutation：YES Mutation：YES ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions 9-12% PEG8000, 100 MM TRIS PH 7.0, 200 MM MGCL2, 80-450 MM SODIUM MALONATE
Resolution 7.60 Å R-free 0.306
5AKD MutS in complex with the N-terminal domain of MutL - crystal form 3 Deposited 2015-03-03 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 I 1–800（800 aa）
Chain J 1–800（800 aa）
Mutation：YES Mutation：YES ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions 9-12% PEG8000, 100 MM TRIS PH 7.0, 200 MM MGCL2, 80-450 MM SODIUM MALONATE
Resolution 7.60 Å R-free 0.306
6I5F Crystal structure of DNA-free E.coli MutS P839E dimer mutant Deposited 2018-11-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–853（853 aa）
Chain B 1–853（853 aa）
Not recorded GOL GLYCEROL × 13 SO4 SULFATE ION × 9 ADP ADENOSINE-5'-DIPHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；297 K；0.1 M Hepes 7.0 7 % Dioxone 1.4 M Ammonium Sulfate
Resolution 2.60 Å R-free 0.257
7AI6 MutS in mismatch bound state Deposited 2020-09-26 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 1–853（853 aa）
Chain B 1–853（853 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE；blot for 3 seconds before plunging
Resolution 6.90 Å
7AI7 MutS in Intermediate state Deposited 2020-09-26 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 1–853（853 aa）
Chain B 1–853（853 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE；blot for 3 seconds before plunging
Resolution 3.90 Å
7AIB MutS-MutL in clamp state Deposited 2020-09-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Heteromer；Protein × 3 PDB declaration: pentameric
Chain A 1–853（853 aa）
Chain B 1–853（853 aa）
Mutation：D825R,C93A,C235S,C239A,C297S,C569S,C711V,D246C Mutation：D825R,C93A,C235S,C239A,C297S,C569S,C711V,D246C ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE；blot for 3 seconds before plunging
Resolution 4.70 Å
7AIC MutS-MutL in clamp state (kinked clamp domain) Deposited 2020-09-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Heteromer；Protein × 3 PDB declaration: pentameric
Chain A 1–853（853 aa）
Chain B 1–853（853 aa）
Mutation：D825R, C93A, C235S, C239A, C297S, C569S, C711V, D246C Mutation：D825R, C93A, C235S, C239A, C297S, C569S, C711V, D246C ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE；blot for 3 seconds before plunging
Resolution 5.00 Å
7OTO The structure of MutS bound to two molecules of AMPPNP Deposited 2021-06-10 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 × 2 PDB declaration: dimeric
Chain A 1–800（800 aa）
Chain B 1–800（800 aa）
Not recorded MG MAGNESIUM ION × 2 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
7OU0 The structure of MutS bound to two molecules of ADP-Vanadate Deposited 2021-06-10 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 × 2 PDB declaration: dimeric
Chain A 1–799（799 aa）
Chain B 1–799（799 aa）
Mutation：R840E Mutation：R840E MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 VO4 VANADATE ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.80 Å
7OU4 The structure of MutS bound to one molecule of ATP and one molecule of ADP Deposited 2021-06-11 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 × 2 PDB declaration: dimeric
Chain A 1–800（800 aa）
Chain B 1–800（800 aa）
Not recorded MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å

24 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MUTS_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–799； UniProt 2–800 Author chain B； PDBConstruct 1–799； UniProt 2–800

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

SAXS profile for 3k0s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3k0s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3k0s
Deposition date deposition_date2009-09-25
Structure title titleCrystal structure of E.coli DNA mismatch repair protein MutS, D693N mutant, in complex with GT mismatched DNA
Keywords keywords;Magnesium mutant, DNA repair protein, Protein-DNA complex, ATP-binding, DNA damage, DNA repair, DNA-binding, Nucleotide-binding, DNA BINDING PROTEIN-DNA complex ;; DNA BINDING PROTEIN/DNA
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier40.61 Å
Radius of gyration Rg (electron density) rg_electron39.99 Å
Forward intensity I(0) i0552439000.00
Molecular weight molecular_weight184040.0 kDa
Excluded volume excluded_volume227150 ų
Envelope volume envelope_volume316940 ų
Hydration-shell volume shell_volume64433 ų
Envelope diameter envelope_diameter131.9 Å
Shell Rg shell_rg47.45 Å
Envelope Rg envelope_rg38.83 Å
Shape Rg shape_rg40.00 Å
Total Rg total_rg40.35 Å
Total atoms total_atoms12892
Residues n_residues1575
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax131.0 Å
Rg (real space) rg_real40.48 Å
Rg uncertainty (real space) rg_real_error1.16 Å
I(0) (real space) i0_real5.5240e+08
I(0) uncertainty (real space) i0_real_error9.8190e+06
Rg (reciprocal space) rg_reciprocal40.61 Å
I(0) (reciprocal space) i0_reciprocal552500000.0000
Solution quality estimate total_estimate0.8274
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary50.4 Å
Skewness Skewness skewness0.163
Kurtosis Kurtosis kurtosis-0.508
Angular range angular_range— – 0.1950 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha46840000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.918; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

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7. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

Domain ID domain_id3k0sA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1170 — MutS, DNA mismatch repair protein, domain I
Homologous superfamily homologous superfamily10 — DNA repair protein MutS, domain I
Domain ID domain_id3k0sA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily110 — MutS, connector domain
Domain ID domain_id3k0sA03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1420 — MutS, DNA mismatch repair protein; Chain A, domain 3
Homologous superfamily homologous superfamily10 —
Domain ID domain_id3k0sA04
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1420 — MutS, DNA mismatch repair protein; Chain A, domain 3
Homologous superfamily homologous superfamily10 —
Domain ID domain_id3k0sA05
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id3k0sB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1170 — MutS, DNA mismatch repair protein, domain I
Homologous superfamily homologous superfamily10 — DNA repair protein MutS, domain I
Domain ID domain_id3k0sB02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily110 — MutS, connector domain
Domain ID domain_id3k0sB03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1420 — MutS, DNA mismatch repair protein; Chain A, domain 3
Homologous superfamily homologous superfamily10 —
Domain ID domain_id3k0sB04
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1420 — MutS, DNA mismatch repair protein; Chain A, domain 3
Homologous superfamily homologous superfamily10 —
Domain ID domain_id3k0sB05
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
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8. Citations (1)

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9. Files and Curves (10)