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1h7u

hPMS2-ATPgS

Method: X-RAY DIFFRACTION Dmax: 104.7 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

MISMATCH REPAIR ENDONUCLEASE PMS2

HOMO SAPIENS

UniProt P54278

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–365 Fragment：GHL ATPASE, RESIDUES 1-365 MG MAGNESIUM ION × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.2；2-2.4 M NA/K PHOSPHATE (PH=6.2) 0.2 M LICL, pH 6.20 Resolution 2.70 Å R-free 0.270
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain B； UniProt 1–365 Fragment：GHL ATPASE, RESIDUES 1-365 MG MAGNESIUM ION × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.2；2-2.4 M NA/K PHOSPHATE (PH=6.2) 0.2 M LICL, pH 6.20 Resolution 2.70 Å R-free 0.270

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 1H7U Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1EA6 N-terminal 40kDa fragment of NhPMS2 complexed with ADP Deposited 2001-07-10 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–364（364 aa） Fragment：N-TERMINAL 40KDA, RESIDUES 1-364
Not recorded MG MAGNESIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.2；2-2.4 M NA/K PHOSPHATE (PH 6.2) 0.2 M LICL
Resolution 2.70 Å R-free 0.262
1EA6 N-terminal 40kDa fragment of NhPMS2 complexed with ADP Deposited 2001-07-10 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1–364（364 aa） Fragment：N-TERMINAL 40KDA, RESIDUES 1-364
Not recorded MG MAGNESIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.2；2-2.4 M NA/K PHOSPHATE (PH 6.2) 0.2 M LICL
Resolution 2.70 Å R-free 0.262
1H7S N-terminal 40kDa fragment of human PMS2 Deposited 2001-07-10 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–365（365 aa） Fragment：N-TERMINAL 40 KDA FRAGMENT
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.2；2-2.4 M NA/K PHOSPHATE (PH 6.2) 0.2 M LICL
Resolution 1.95 Å R-free 0.243
1H7S N-terminal 40kDa fragment of human PMS2 Deposited 2001-07-10 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1–365（365 aa） Fragment：N-TERMINAL 40 KDA FRAGMENT
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.2；2-2.4 M NA/K PHOSPHATE (PH 6.2) 0.2 M LICL
Resolution 1.95 Å R-free 0.243
5U5R Crystal Structure and X-ray Diffraction Data Collection of Importin-alpha from Mus musculus Complexed with a PMS2 NLS Peptide Deposited 2016-12-07 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 573–583（11 aa）
Not recorded DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.600-0.625 M sodium citrate (pH 6) and 10 mM DTT
Resolution 2.10 Å R-free 0.207
6MFQ Crystal structure of a PMS2 variant Deposited 2018-09-11 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–365（365 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；289.15 K；Crystals were obtained in conditions containing 4% tacsimate pH 5 (v/v) and 25% PEG 3350 (w/v). The concentrated PMS2 G207E protein (7 mg/mL) was combined with 0.1ul of an additive (0.1 M calcium chloride dehydrate) prior to the addition of crystallization reagent in a 1:1 ratio.
Resolution 2.60 Å R-free 0.232
6MFQ Crystal structure of a PMS2 variant Deposited 2018-09-11 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1–365（365 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；289.15 K；Crystals were obtained in conditions containing 4% tacsimate pH 5 (v/v) and 25% PEG 3350 (w/v). The concentrated PMS2 G207E protein (7 mg/mL) was combined with 0.1ul of an additive (0.1 M calcium chloride dehydrate) prior to the addition of crystallization reagent in a 1:1 ratio.
Resolution 2.60 Å R-free 0.232
7RCB Crystal Structure of a PMS2 VUS Deposited 2021-07-07 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 1–365（365 aa）
Chain B 1–365（365 aa）
Mutation：N335S Mutation：N335S No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.8；289.15 K；1:1 7.5 mg/mL protein with 8% v/v Tacsimate, pH 5.8, 25% w/v PEG3350
Resolution 2.00 Å R-free 0.198
7RCI Crystal Structure of a PMS2 VUS with Substrate Deposited 2021-07-07 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 1–365（365 aa）
Chain B 1–365（365 aa）
Mutation：N335S Mutation：N335S ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.8；289.15 K；1:1 7.5 mg/mL protein with 8% v/v Tacsimate, pH 5.8, 25% w/v PEG3350
Resolution 2.12 Å R-free 0.248
7RCK Crystal Structure of PMS2 with Substrate Deposited 2021-07-07 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 1–365（365 aa）
Chain B 1–365（365 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.8；289.15 K；1:1 7.5 mg/mL protein with 8% v/v Tacsimate, pH 5.8, 25% w/v PEG3350
Resolution 2.04 Å R-free 0.234
9S89 N-terminal 40kDa fragment of human PMS2 with covalent ligand NP1867 Deposited 2025-08-05 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–365（365 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å R-free 0.229

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

View Construct and Data Evidence
UniProt name PMS2_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–365； UniProt 1–365 Author chain B； PDBConstruct 1–365； UniProt 1–365

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 1h7u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1h7u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1h7u
Deposition date deposition_date2001-07-10
Structure title titlehPMS2-ATPgS
Keywords keywordsDNA REPAIR, GHL ATPASE; DNA REPAIR
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_guinier28.70 Å
Radius of gyration Rg (electron density) rg_electron28.22 Å
Forward intensity I(0) i078896000.00
Molecular weight molecular_weight68326.0 kDa
Excluded volume excluded_volume85067 ų
Envelope volume envelope_volume106640 ų
Hydration-shell volume shell_volume32445 ų
Envelope diameter envelope_diameter111.0 Å
Shell Rg shell_rg34.30 Å
Envelope Rg envelope_rg28.55 Å
Shape Rg shape_rg28.22 Å
Total Rg total_rg28.83 Å
Total atoms total_atoms4777
Residues n_residues610
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 dmax104.7 Å
Rg (real space) rg_real28.76 Å
Rg uncertainty (real space) rg_real_error0.98 Å
I(0) (real space) i0_real7.8900e+07
I(0) uncertainty (real space) i0_real_error1.3180e+06
Rg (reciprocal space) rg_reciprocal28.73 Å
I(0) (reciprocal space) i0_reciprocal78890000.0000
Solution quality estimate total_estimate0.8333
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary102.8 Å
Skewness Skewness skewness0.494
Kurtosis Kurtosis kurtosis0.203
Angular range angular_range— – 0.2750 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15590000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.663; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.873; Smooth: 0.965
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1h7ua1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.14 — Ribosomal protein S5 domain 2-like
Superfamily Superfamily superfamilyd.14.1 — Ribosomal protein S5 domain 2-like
Family Family familyd.14.1.3 — DNA gyrase/MutL, second domain
Domain ID domain_idd1h7ua2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.122 — ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
Superfamily Superfamily superfamilyd.122.1 — ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
Family Family familyd.122.1.2 — DNA gyrase/MutL, N-terminal domain
Domain ID domain_idd1h7ub1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.14 — Ribosomal protein S5 domain 2-like
Superfamily Superfamily superfamilyd.14.1 — Ribosomal protein S5 domain 2-like
Family Family familyd.14.1.3 — DNA gyrase/MutL, second domain
Domain ID domain_idd1h7ub2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.122 — ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
Superfamily Superfamily superfamilyd.122.1 — ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
Family Family familyd.122.1.2 — DNA gyrase/MutL, N-terminal domain

CATH v4.4 (4 domains)

Domain ID domain_id1h7uA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology565 — Heat Shock Protein 90
Homologous superfamily homologous superfamily10 — Histidine kinase-like ATPase, C-terminal domain
Domain ID domain_id1h7uA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology230 — Ribosomal Protein S5; domain 2
Homologous superfamily homologous superfamily10 —
Domain ID domain_id1h7uB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology565 — Heat Shock Protein 90
Homologous superfamily homologous superfamily10 — Histidine kinase-like ATPase, C-terminal domain
Domain ID domain_id1h7uB02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology230 — Ribosomal Protein S5; domain 2
Homologous superfamily homologous superfamily10 —
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8. Citations (1)

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9. Files and Curves (10)