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7aib

MutS-MutL in clamp state

Method: ELECTRON MICROSCOPY Dmax: 126.8 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

DNA mismatch repair protein MutS

Escherichia coli (strain K12)

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 Heteromer Protein × 3 DNA 2 PDB declaration: pentameric（5） Consistent with all polymer counts Chain A； UniProt 1–853 Chain B； UniProt 1–853 Mutation：D825R,C93A,C235S,C239A,C297S,C569S,C711V,D246C DNA mismatch repair protein MutL × 1 （P23367） DNA (30-MER) × 1 DNA (30-MER) × 1 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

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 7AIB 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 oligomeric state 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 1–800（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 oligomeric state 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 1–800（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 oligomeric state 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 1–800（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 oligomeric state 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 1–800（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 oligomeric state 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 1–800（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 oligomeric state 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 1–800（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 oligomeric state 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 1–800（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 oligomeric state 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 1–800（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 oligomeric state 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 1–800（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 oligomeric state 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 1–800（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 method 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 oligomeric state 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 1–800（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
3K0S Crystal structure of E.coli DNA mismatch repair protein MutS, D693N mutant, in complex with GT mismatched DNA Deposited 2009-09-25 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 Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 2–800（799 aa） Fragment：UNP residues 2-800
Chain B 2–800（799 aa） Fragment：UNP residues 2-800
Mutation：D693N Mutation：D693N 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
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 method 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 method 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 experimental method 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 experimental method 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 experimental method 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 experimental method 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 experimental method 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 experimental method 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 experimental method 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 experimental method 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 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 1–853（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 mutation/modification Different oligomeric state Different ligand/ion 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 mutation/modification Different oligomeric state Different ligand/ion 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
7AIC MutS-MutL in clamp state (kinked clamp domain) Deposited 2020-09-26 Different mutation/modification 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 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 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 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 1–853； UniProt 1–853 Author chain B； PDBConstruct 1–853； UniProt 1–853

DNA mismatch repair protein MutL

Escherichia coli (strain K12)

UniProt P23367

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 Heteromer Protein × 3 DNA 2 PDB declaration: pentameric（5） Consistent with all polymer counts Chain C； UniProt 1–331 Mutation：N131C,C61S,C216L,C256F,C276Y DNA mismatch repair protein MutS × 2 （P23909） DNA (30-MER) × 1 DNA (30-MER) × 1 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

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 7AIB Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1B62 MUTL COMPLEXED WITH ADP Deposited 1999-01-11 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 1–349（349 aa） Fragment：ATPASE FRAGMENT
Not recorded MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5；pH 8.5
Resolution 2.10 Å R-free 0.253
1B63 MUTL COMPLEXED WITH ADPNP Deposited 1999-01-20 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 1–331（331 aa） Fragment：ATPASE FRAGMENT
Not recorded MG MAGNESIUM ION × 2 EDO 1,2-ETHANEDIOL × 4 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5；pH 8.5
Resolution 1.90 Å R-free 0.261
1BKN CRYSTAL STRUCTURE OF AN N-TERMINAL 40KD FRAGMENT OF E. COLI DNA MISMATCH REPAIR PROTEIN MUTL Deposited 1998-07-09 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 1–349（349 aa） Fragment：N-TERMINAL 40KD FRAGMENT
Chain B 1–349（349 aa） Fragment：N-TERMINAL 40KD FRAGMENT
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.6；pH 6.6
Resolution 2.90 Å R-free 0.300
1X9Z Crystal structure of the MutL C-terminal domain Deposited 2004-08-24 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 432–615（184 aa） Fragment：C-terminal domain
Chain B 432–615（184 aa） Fragment：C-terminal domain
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 2 NA SODIUM ION × 1 GOL GLYCEROL × 2 IPA ISOPROPYL ALCOHOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 4.6；277 K；NaCl, Li2SO4, sodium acetate, pH 4.6, VAPOR DIFFUSION, temperature 277K
Resolution 2.10 Å R-free 0.278
1X9Z Crystal structure of the MutL C-terminal domain Deposited 2004-08-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 432–615（184 aa） Fragment：C-terminal domain
Chain B 432–615（184 aa） Fragment：C-terminal domain
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 4 NA SODIUM ION × 2 GOL GLYCEROL × 4 IPA ISOPROPYL ALCOHOL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 4.6；277 K；NaCl, Li2SO4, sodium acetate, pH 4.6, VAPOR DIFFUSION, temperature 277K
Resolution 2.10 Å R-free 0.278
1X9Z Crystal structure of the MutL C-terminal domain Deposited 2004-08-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 432–615（184 aa） Fragment：C-terminal domain
Chain B 432–615（184 aa） Fragment：C-terminal domain
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 4 NA SODIUM ION × 2 GOL GLYCEROL × 4 IPA ISOPROPYL ALCOHOL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 4.6；277 K；NaCl, Li2SO4, sodium acetate, pH 4.6, VAPOR DIFFUSION, temperature 277K
Resolution 2.10 Å R-free 0.278
1X9Z Crystal structure of the MutL C-terminal domain Deposited 2004-08-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 432–615（184 aa） Fragment：C-terminal domain
Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 4 NA SODIUM ION × 2 GOL GLYCEROL × 2 IPA ISOPROPYL ALCOHOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 4.6；277 K；NaCl, Li2SO4, sodium acetate, pH 4.6, VAPOR DIFFUSION, temperature 277K
Resolution 2.10 Å R-free 0.278
1X9Z Crystal structure of the MutL C-terminal domain Deposited 2004-08-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 5 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain B 432–615（184 aa） Fragment：C-terminal domain
Non-standard monomer：Yes (specific site not provided by mmCIF) GOL GLYCEROL × 2 IPA ISOPROPYL ALCOHOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 4.6；277 K；NaCl, Li2SO4, sodium acetate, pH 4.6, VAPOR DIFFUSION, temperature 277K
Resolution 2.10 Å R-free 0.278
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 experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 1–349（349 aa） Fragment：N-TERMINAL DOMAIN
Chain D 1–349（349 aa） Fragment：N-TERMINAL DOMAIN
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 experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain F 1–349（349 aa） Fragment：N-TERMINAL DOMAIN
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 experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 1–349（349 aa） Fragment：N-TERMINAL DOMAIN
Chain D 1–349（349 aa） Fragment：N-TERMINAL DOMAIN
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 experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain G 1–349（349 aa） Fragment：N-TERMINAL DOMAIN
Chain H 1–349（349 aa） Fragment：N-TERMINAL DOMAIN
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 experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain K 1–349（349 aa） Fragment：N-TERMINAL DOMAIN
Chain L 1–349（349 aa） Fragment：N-TERMINAL DOMAIN
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 experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 1–349（349 aa） Fragment：N-TERMINAL DOMAIN, RESIDUES 1-349
Chain D 1–349（349 aa） Fragment：N-TERMINAL DOMAIN, RESIDUES 1-349
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 experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain G 1–349（349 aa） Fragment：N-TERMINAL DOMAIN, RESIDUES 1-349
Chain H 1–349（349 aa） Fragment：N-TERMINAL DOMAIN, RESIDUES 1-349
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 experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain K 1–349（349 aa） Fragment：N-TERMINAL DOMAIN, RESIDUES 1-349
Chain L 1–349（349 aa） Fragment：N-TERMINAL DOMAIN, RESIDUES 1-349
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
7AIC MutS-MutL in clamp state (kinked clamp domain) Deposited 2020-09-26 Different structure-quality metrics Assembly 1 Protein–DNA Heteromer；Protein × 3 PDB declaration: pentameric
Chain C 1–331（331 aa）
Mutation：N131C,C61S,C216L,C256F,C276Y 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
7P8V The structure of E. coli MutL bound to a 3' resected DNA end Deposited 2021-07-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 1–615（615 aa）
Chain B 1–615（615 aa）
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
9PRP N-terminal domain of E. coli MutL bound to NP660 Deposited 2025-07-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–349（349 aa）
Not recorded A1CKR 5-(cyclopentyloxy)benzene-1,3-diol × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；295 K；21% PEG3350, 200 mM ammonium tartrate, 100 mM Bis-Tris, pH 6.0
Resolution 2.10 Å R-free 0.295
9PRP N-terminal domain of E. coli MutL bound to NP660 Deposited 2025-07-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1–349（349 aa）
Not recorded A1CKR 5-(cyclopentyloxy)benzene-1,3-diol × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；295 K；21% PEG3350, 200 mM ammonium tartrate, 100 mM Bis-Tris, pH 6.0
Resolution 2.10 Å R-free 0.295

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

View Construct and Data Evidence
UniProt name MUTL_ECOLI
Isoform —
PDB entities 2
Chains and sequence ranges Author chain C； PDBConstruct 21–351； UniProt 1–331

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 7aib

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7aib
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7aib
Deposition date deposition_date2020-09-26
Structure title titleMutS-MutL in clamp state
Keywords keywordsDNA Mismatch Repair MutS, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier40.27 Å
Radius of gyration Rg (electron density) rg_electron40.01 Å
Forward intensity I(0) i0674183000.00
Molecular weight molecular_weight197840.0 kDa
Excluded volume excluded_volume241890 ų
Envelope volume envelope_volume347620 ų
Hydration-shell volume shell_volume70611 ų
Envelope diameter envelope_diameter127.0 Å
Shell Rg shell_rg47.24 Å
Envelope Rg envelope_rg39.40 Å
Shape Rg shape_rg40.05 Å
Total Rg total_rg40.26 Å
Total atoms total_atoms13839
Residues n_residues1651
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 dmax126.8 Å
Rg (real space) rg_real40.11 Å
Rg uncertainty (real space) rg_real_error0.99 Å
I(0) (real space) i0_real6.7420e+08
I(0) uncertainty (real space) i0_real_error1.1400e+07
Rg (reciprocal space) rg_reciprocal40.27 Å
I(0) (reciprocal space) i0_reciprocal674300000.0000
Solution quality estimate total_estimate0.8961
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.8 Å
Skewness Skewness skewness0.162
Kurtosis Kurtosis kurtosis-0.489
Angular range angular_range— – 0.1950 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha53500000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.914; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.919
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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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8. Citations (1)

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9. Files and Curves (10)