Current Protein Identity：Q13257
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Difference tags compare only the current result set; every original PDB and assembly record remains separate.
Related-Structure Differences
Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.
| PDB Entry | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Experimental Method | Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 1DUJ SOLUTION STRUCTURE OF THE SPINDLE ASSEMBLY CHECKPOINT PROTEIN HUMAN MAD2 Deposited 2000-01-17 | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain A
11–195（185 aa）
Fragment：FULL PROTEIN WITHOUT BOTH N- AND C-TERMINAL 10 RESIDUES
|
Not recorded | No recorded non-water small molecule | SOLUTION NMR |
NMR measurement conditions
pH 6.8；303 K；Ionic strength (raw mmCIF value) 300mM KCl；Pressure ambient
NMR measurement conditions
pH 6.8；303 K；Ionic strength (raw mmCIF value) 300mM KCl；Pressure ambient
NMR measurement conditions
pH 6.8；303 K；Ionic strength (raw mmCIF value) 300mM KCl；Pressure ambient
NMR measurement conditions
pH 6.8；303 K；Ionic strength (raw mmCIF value) 300mM KCl；Pressure ambient
NMR measurement conditions
pH 6.8；303 K；Ionic strength (raw mmCIF value) 300mM KCl；Pressure ambient
NMR sample composition
1.2mM Mad2 protein U-15N,13C,2H; 50mM sodium phosphate (pH 6.8), 300mM KCl, 5mM DTT, 0.04% NaN3; 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition
1.4mM Mad2 protein U-15N,13C; U-60% 2H; 50mM sodium phosphate (pH 6.8), 300mM KCl, 5mM DTT, 0.04% NaN3; 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition
1.5mM Mad2 protein U-15N; 50mM sodium phosphate (pH 6.8), 300mM KCl, 5mM DTT, 0.04% NaN3; 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition
1.6mM Mad2 protein U-10% 13C; 50mM sodium phosphate (pH 6.8), 300mM KCl, 5mM DTT, 0.04% NaN3; 100% D2O | 100% D2O
NMR sample composition
1.7mM Mad2 protein U-15N,13C; 50mM sodium phosphate (pH 6.8), 300mM KCl, 5mM DTT, 0.04% NaN3; 100% D2O | 100% D2O
|
Resolution not provided |
| 1GO4 Crystal structure of Mad1-Mad2 reveals a conserved Mad2 binding motif in Mad1 and Cdc20. Deposited 2001-10-17 | Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count |
Chain A
1–205（205 aa）
Chain B
1–205（205 aa）
Chain C
1–205（205 aa）
Chain D
1–205（205 aa）
|
Mutation：R133A Mutation：R133A Mutation：R133A Mutation：R133A | No recorded non-water small molecule | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.2；PROTEIN CONCENTRATION 7.5 MG/ML HANGING DROP METHOD, WELL=100 MM AMMONIUM SULPHATE, 100 MM AMMONIUM CITRATE PH 5.2, 10 MM DTT
|
Resolution 2.05 Å R-free 0.268 |
| 1KLQ The Mad2 Spindle Checkpoint Protein Undergoes Similar Major Conformational Changes upon Binding to Either Mad1 or Cdc20 Deposited 2001-12-12 | Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
Chain A
9–205（197 aa）
Fragment：MISSING N-TERMINAL 10 RESIDUES
|
Not recorded | No recorded non-water small molecule | SOLUTION NMR |
NMR measurement conditions
pH 7.4；303 K；Ionic strength (raw mmCIF value) 0.3M KCl；Pressure ambient
NMR measurement conditions
pH 7.4；303 K；Ionic strength (raw mmCIF value) 0.3M KCl；Pressure ambient
NMR measurement conditions
pH 7.4；303 K；Ionic strength (raw mmCIF value) 0.3M KCl；Pressure ambient
NMR measurement conditions
pH 7.4；303 K；Ionic strength (raw mmCIF value) 0.3M KCl；Pressure ambient
NMR measurement conditions
pH 7.4；303 K；Ionic strength (raw mmCIF value) 0.3M KCl；Pressure ambient
NMR measurement conditions
pH 7.4；303 K；Ionic strength (raw mmCIF value) 0.3M KCl；Pressure ambient
NMR sample composition
0.8mM Mad2 protein U-15N; 1mM MBP1 NA;
50mM phosphate buffer; 0.3M KCl;
1mM DTT | 90% H2O/10% D2O
NMR sample composition
0.8mM Mad2 protein U-15N, 13C, 2H; 1mM MBP1 NA;
50mM phosphate buffer; 0.3M KCl;
1mM DTT | 90% H2O/10% D2O
NMR sample composition
0.8mM Mad2 protein U-15N, 13C; 1mM MBP1 NA;
50mM phosphate buffer; 0.3M KCl;
1mM DTT | 90% H2O/10% D2O
NMR sample composition
0.8mM Mad2 protein U-15N, 13C, U-60% 2H; 1mM MBP1 NA;
50mM phosphate buffer; 0.3M KCl;
1mM DTT | 90% H2O/10% D2O
NMR sample composition
0.8mM MBP1 U-15N; 1mM Mad2 protein NA;
50mM phosphate buffer; 0.3M KCl;
1mM DTT | 90% H2O/10% D2O
NMR sample composition
0.8mM MBP1 U-15N, 13C; 1mM Mad2 protein NA;
50mM phosphate buffer; 0.3M KCl;
1mM DTT | 90% H2O/10% D2O
|
Resolution not provided |
| 1S2H The Mad2 spindle checkpoint protein possesses two distinct natively folded states Deposited 2004-01-08 | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain A
1–205（205 aa）
|
Mutation：R133A | No recorded non-water small molecule | SOLUTION NMR |
NMR measurement conditions
pH 6.8；303 K；Ionic strength (raw mmCIF value) 0.3M KCl；Pressure ambient
NMR sample composition
0.8mM Mad2 protein U-15N,13C,2H | 90% H2O, 10% D2O; 50mM phosphate buffer;
0.3M KCl; 1mM DTT
NMR sample composition
0.8mM Mad2 protein U-15N | 90% H2O, 10% D2O; 50mM phosphate buffer;
0.3M KCl; 1mM DTT
NMR sample composition
0.8mM Mad2 protein U-15N,13C | 90% H2O, 10% D2O; 50mM phosphate buffer;
0.3M KCl; 1mM DTT
|
Resolution not provided |
| 2QYF Crystal structure of the Mad2/p31(comet)/Mad2-binding peptide ternary complex Deposited 2007-08-14 | Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
1–205（205 aa）
|
Mutation：L13A Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5；289 K；16% (w/v) PEG 3350, 16% (v/v) glycerol, 125 mM sodium phosphate (pH 5.0), 100 mM NaCl, 25 mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 289K
|
Resolution 2.30 Å R-free 0.257 |
| 2QYF Crystal structure of the Mad2/p31(comet)/Mad2-binding peptide ternary complex Deposited 2007-08-14 | Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain C
1–205（205 aa）
|
Mutation：L13A Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5；289 K；16% (w/v) PEG 3350, 16% (v/v) glycerol, 125 mM sodium phosphate (pH 5.0), 100 mM NaCl, 25 mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 289K
|
Resolution 2.30 Å R-free 0.257 |
| 2V64 Crystallographic structure of the conformational dimer of the Spindle Assembly Checkpoint protein Mad2. Deposited 2007-07-13 | Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
2–205（204 aa）
Fragment：RESIDUES 2-205
Chain E
2–108（107 aa）
Fragment：RESIDUES 2-108,118-205
Chain E
118–205（88 aa）
Fragment：RESIDUES 2-108,118-205
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION |
X-ray crystallization conditions
pH 4.6；0.1M NAACETATE PH 4.6, 3.5M NAFORMATE
|
Resolution 2.90 Å R-free 0.273 |
| 2V64 Crystallographic structure of the conformational dimer of the Spindle Assembly Checkpoint protein Mad2. Deposited 2007-07-13 | Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain C
2–205（204 aa）
Fragment：RESIDUES 2-205
Chain D
2–108（107 aa）
Fragment：RESIDUES 2-108,118-205
Chain D
118–205（88 aa）
Fragment：RESIDUES 2-108,118-205
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION |
X-ray crystallization conditions
pH 4.6；0.1M NAACETATE PH 4.6, 3.5M NAFORMATE
|
Resolution 2.90 Å R-free 0.273 |
| 2V64 Crystallographic structure of the conformational dimer of the Spindle Assembly Checkpoint protein Mad2. Deposited 2007-07-13 | Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain F
2–205（204 aa）
Fragment：RESIDUES 2-205
Chain H
2–108（107 aa）
Fragment：RESIDUES 2-108,118-205
Chain H
118–205（88 aa）
Fragment：RESIDUES 2-108,118-205
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION |
X-ray crystallization conditions
pH 4.6；0.1M NAACETATE PH 4.6, 3.5M NAFORMATE
|
Resolution 2.90 Å R-free 0.273 |
| 2VFX Structure of the Symmetric Mad2 Dimer Deposited 2007-11-05 | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain A
1–205（205 aa）
|
Mutation：YES | MG MAGNESIUM ION × 1 CL CHLORIDE ION × 3 PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；VAPOR DIFFUSION, HANGING DROP, 20 DEGREES C. 1 MICROLITER PROTEIN: 3 MG/ML IN 20 MM TRIS, PH 8.0, 50 MM NACL, 2 MM TCEP PLUS 1 MICROLITER RESERVOIR: 19% PEG2000, 16% GLYCEROL, 100 MM TRIS, PH 8.0, 0.3 M MGCL2
|
Resolution 1.95 Å R-free 0.247 |
| 2VFX Structure of the Symmetric Mad2 Dimer Deposited 2007-11-05 | Assembly 10 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain J
1–205（205 aa）
|
Mutation：YES | CL CHLORIDE ION × 5 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；VAPOR DIFFUSION, HANGING DROP, 20 DEGREES C. 1 MICROLITER PROTEIN: 3 MG/ML IN 20 MM TRIS, PH 8.0, 50 MM NACL, 2 MM TCEP PLUS 1 MICROLITER RESERVOIR: 19% PEG2000, 16% GLYCEROL, 100 MM TRIS, PH 8.0, 0.3 M MGCL2
|
Resolution 1.95 Å R-free 0.247 |
| 2VFX Structure of the Symmetric Mad2 Dimer Deposited 2007-11-05 | Assembly 11 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain K
1–205（205 aa）
|
Mutation：YES | MG MAGNESIUM ION × 1 CL CHLORIDE ION × 2 PE3 3,6,9,12,15,18,21,24,27,30,33,36,39-TRIDECAOXAHENTETRACONTANE-1,41-DIOL × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；VAPOR DIFFUSION, HANGING DROP, 20 DEGREES C. 1 MICROLITER PROTEIN: 3 MG/ML IN 20 MM TRIS, PH 8.0, 50 MM NACL, 2 MM TCEP PLUS 1 MICROLITER RESERVOIR: 19% PEG2000, 16% GLYCEROL, 100 MM TRIS, PH 8.0, 0.3 M MGCL2
|
Resolution 1.95 Å R-free 0.247 |
| 2VFX Structure of the Symmetric Mad2 Dimer Deposited 2007-11-05 | Assembly 12 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain L
1–205（205 aa）
|
Mutation：YES | MG MAGNESIUM ION × 1 CL CHLORIDE ION × 3 PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；VAPOR DIFFUSION, HANGING DROP, 20 DEGREES C. 1 MICROLITER PROTEIN: 3 MG/ML IN 20 MM TRIS, PH 8.0, 50 MM NACL, 2 MM TCEP PLUS 1 MICROLITER RESERVOIR: 19% PEG2000, 16% GLYCEROL, 100 MM TRIS, PH 8.0, 0.3 M MGCL2
|
Resolution 1.95 Å R-free 0.247 |
| 2VFX Structure of the Symmetric Mad2 Dimer Deposited 2007-11-05 | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain B
1–205（205 aa）
|
Mutation：YES | MG MAGNESIUM ION × 1 CL CHLORIDE ION × 4 PE3 3,6,9,12,15,18,21,24,27,30,33,36,39-TRIDECAOXAHENTETRACONTANE-1,41-DIOL × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；VAPOR DIFFUSION, HANGING DROP, 20 DEGREES C. 1 MICROLITER PROTEIN: 3 MG/ML IN 20 MM TRIS, PH 8.0, 50 MM NACL, 2 MM TCEP PLUS 1 MICROLITER RESERVOIR: 19% PEG2000, 16% GLYCEROL, 100 MM TRIS, PH 8.0, 0.3 M MGCL2
|
Resolution 1.95 Å R-free 0.247 |
| 2VFX Structure of the Symmetric Mad2 Dimer Deposited 2007-11-05 | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain C
1–205（205 aa）
|
Mutation：YES | MG MAGNESIUM ION × 1 CL CHLORIDE ION × 3 PE3 3,6,9,12,15,18,21,24,27,30,33,36,39-TRIDECAOXAHENTETRACONTANE-1,41-DIOL × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；VAPOR DIFFUSION, HANGING DROP, 20 DEGREES C. 1 MICROLITER PROTEIN: 3 MG/ML IN 20 MM TRIS, PH 8.0, 50 MM NACL, 2 MM TCEP PLUS 1 MICROLITER RESERVOIR: 19% PEG2000, 16% GLYCEROL, 100 MM TRIS, PH 8.0, 0.3 M MGCL2
|
Resolution 1.95 Å R-free 0.247 |
| 2VFX Structure of the Symmetric Mad2 Dimer Deposited 2007-11-05 | Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain D
1–205（205 aa）
|
Mutation：YES | CL CHLORIDE ION × 5 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；VAPOR DIFFUSION, HANGING DROP, 20 DEGREES C. 1 MICROLITER PROTEIN: 3 MG/ML IN 20 MM TRIS, PH 8.0, 50 MM NACL, 2 MM TCEP PLUS 1 MICROLITER RESERVOIR: 19% PEG2000, 16% GLYCEROL, 100 MM TRIS, PH 8.0, 0.3 M MGCL2
|
Resolution 1.95 Å R-free 0.247 |
| 2VFX Structure of the Symmetric Mad2 Dimer Deposited 2007-11-05 | Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain E
1–205（205 aa）
|
Mutation：YES | MG MAGNESIUM ION × 1 CL CHLORIDE ION × 5 PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；VAPOR DIFFUSION, HANGING DROP, 20 DEGREES C. 1 MICROLITER PROTEIN: 3 MG/ML IN 20 MM TRIS, PH 8.0, 50 MM NACL, 2 MM TCEP PLUS 1 MICROLITER RESERVOIR: 19% PEG2000, 16% GLYCEROL, 100 MM TRIS, PH 8.0, 0.3 M MGCL2
|
Resolution 1.95 Å R-free 0.247 |
| 2VFX Structure of the Symmetric Mad2 Dimer Deposited 2007-11-05 | Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain F
1–205（205 aa）
|
Mutation：YES | MG MAGNESIUM ION × 1 CL CHLORIDE ION × 2 PE3 3,6,9,12,15,18,21,24,27,30,33,36,39-TRIDECAOXAHENTETRACONTANE-1,41-DIOL × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；VAPOR DIFFUSION, HANGING DROP, 20 DEGREES C. 1 MICROLITER PROTEIN: 3 MG/ML IN 20 MM TRIS, PH 8.0, 50 MM NACL, 2 MM TCEP PLUS 1 MICROLITER RESERVOIR: 19% PEG2000, 16% GLYCEROL, 100 MM TRIS, PH 8.0, 0.3 M MGCL2
|
Resolution 1.95 Å R-free 0.247 |
| 2VFX Structure of the Symmetric Mad2 Dimer Deposited 2007-11-05 | Assembly 7 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain G
1–205（205 aa）
|
Mutation：YES | MG MAGNESIUM ION × 1 CL CHLORIDE ION × 1 PE3 3,6,9,12,15,18,21,24,27,30,33,36,39-TRIDECAOXAHENTETRACONTANE-1,41-DIOL × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；VAPOR DIFFUSION, HANGING DROP, 20 DEGREES C. 1 MICROLITER PROTEIN: 3 MG/ML IN 20 MM TRIS, PH 8.0, 50 MM NACL, 2 MM TCEP PLUS 1 MICROLITER RESERVOIR: 19% PEG2000, 16% GLYCEROL, 100 MM TRIS, PH 8.0, 0.3 M MGCL2
|
Resolution 1.95 Å R-free 0.247 |
| 2VFX Structure of the Symmetric Mad2 Dimer Deposited 2007-11-05 | Assembly 8 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain H
1–205（205 aa）
|
Mutation：YES | PE3 3,6,9,12,15,18,21,24,27,30,33,36,39-TRIDECAOXAHENTETRACONTANE-1,41-DIOL × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；VAPOR DIFFUSION, HANGING DROP, 20 DEGREES C. 1 MICROLITER PROTEIN: 3 MG/ML IN 20 MM TRIS, PH 8.0, 50 MM NACL, 2 MM TCEP PLUS 1 MICROLITER RESERVOIR: 19% PEG2000, 16% GLYCEROL, 100 MM TRIS, PH 8.0, 0.3 M MGCL2
|
Resolution 1.95 Å R-free 0.247 |
| 2VFX Structure of the Symmetric Mad2 Dimer Deposited 2007-11-05 | Assembly 9 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain I
1–205（205 aa）
|
Mutation：YES | CL CHLORIDE ION × 4 PEG DI(HYDROXYETHYL)ETHER × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；VAPOR DIFFUSION, HANGING DROP, 20 DEGREES C. 1 MICROLITER PROTEIN: 3 MG/ML IN 20 MM TRIS, PH 8.0, 50 MM NACL, 2 MM TCEP PLUS 1 MICROLITER RESERVOIR: 19% PEG2000, 16% GLYCEROL, 100 MM TRIS, PH 8.0, 0.3 M MGCL2
|
Resolution 1.95 Å R-free 0.247 |
| 3GMH Crystal Structure of the Mad2 Dimer Deposited 2009-03-13 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
Chain A
11–205（195 aa）
Chain B
11–205（195 aa）
|
Not recorded | SO4 SULFATE ION × 3 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；1.6M ammonium sulfate, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K
|
Resolution 3.95 Å R-free 0.251 |
| 3GMH Crystal Structure of the Mad2 Dimer Deposited 2009-03-13 | Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
Chain C
11–205（195 aa）
Chain D
11–205（195 aa）
|
Not recorded | SO4 SULFATE ION × 3 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；1.6M ammonium sulfate, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K
|
Resolution 3.95 Å R-free 0.251 |
| 3GMH Crystal Structure of the Mad2 Dimer Deposited 2009-03-13 | Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
Chain E
11–205（195 aa）
Chain F
11–205（195 aa）
|
Not recorded | SO4 SULFATE ION × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；1.6M ammonium sulfate, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K
|
Resolution 3.95 Å R-free 0.251 |
| 3GMH Crystal Structure of the Mad2 Dimer Deposited 2009-03-13 | Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
Chain G
11–205（195 aa）
Chain H
11–205（195 aa）
|
Not recorded | SO4 SULFATE ION × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；1.6M ammonium sulfate, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K
|
Resolution 3.95 Å R-free 0.251 |
| 3GMH Crystal Structure of the Mad2 Dimer Deposited 2009-03-13 | Assembly 5 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
Chain I
11–205（195 aa）
Chain J
11–205（195 aa）
|
Not recorded | SO4 SULFATE ION × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；1.6M ammonium sulfate, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K
|
Resolution 3.95 Å R-free 0.251 |
| 3GMH Crystal Structure of the Mad2 Dimer Deposited 2009-03-13 | Assembly 6 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
Chain K
11–205（195 aa）
Chain L
11–205（195 aa）
|
Not recorded | SO4 SULFATE ION × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；1.6M ammonium sulfate, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K
|
Resolution 3.95 Å R-free 0.251 |
| 5KHU Model of human Anaphase-promoting complex/Cyclosome (APC15 deletion mutant), in complex with the Mitotic checkpoint complex (APC/C-CDC20-MCC) based on cryo EM data at 4.8 Angstrom resolution Deposited 2016-06-15 | Assembly 1 Protein heterocomplex Heteromer；Protein × 23 PDB declaration: 23-meric（23） Consistent with protein count |
Chain T
1–205（205 aa）
|
Not recorded | No recorded non-water small molecule | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 4.80 Å |
| 5LCW Cryo-EM structure of the Anaphase-promoting complex/Cyclosome, in complex with the Mitotic checkpoint complex (APC/C-MCC) at 4.2 angstrom resolution Deposited 2016-06-22 | Assembly 1 Protein heterocomplex Heteromer；Protein × 23 PDB declaration: 23-meric（23） Consistent with protein count |
Chain Z
1–205（205 aa）
|
Not recorded | No recorded non-water small molecule | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 4.20 Å |
| 6F0X Cryo-EM structure of TRIP13 in complex with ATP gamma S, p31comet, C-Mad2 and Cdc20 Deposited 2017-11-20 | Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric（9） Consistent with protein count |
Chain Z
1–205（205 aa）
|
Not recorded | AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 5 | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 4.60 Å |
| 6TLJ Cryo-EM structure of the Anaphase-promoting complex/Cyclosome, in complex with the Mitotic checkpoint complex (APC/C-MCC) at 3.8 angstrom resolution Deposited 2019-12-02 | Assembly 1 Protein heterocomplex Heteromer；Protein × 23 PDB declaration: 23-meric（23） Consistent with protein count |
Chain Z
1–205（205 aa）
|
Not recorded | No recorded non-water small molecule | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.80 Å |