SAXSdb — 7b1h

▼

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

Mitotic spindle assembly checkpoint protein MAD1

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 597–718 Chain B； UniProt 597–718	Not recorded	Mitotic checkpoint serine/threonine-protein kinase BUB1 × 2 （O43683）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；8% Isopropanol, 20% PEG 4000, 0.1 M Na HEPES, pH 7.5	Resolution 2.40 Å R-free 0.281
2	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain E； UniProt 597–718 Chain F； UniProt 597–718	Not recorded	Mitotic checkpoint serine/threonine-protein kinase BUB1 × 2 （O43683）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；8% Isopropanol, 20% PEG 4000, 0.1 M Na HEPES, pH 7.5	Resolution 2.40 Å R-free 0.281

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 7B1H	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1GO4 Crystal structure of Mad1-Mad2 reveals a conserved Mad2 binding motif in Mad1 and Cdc20. Deposited 2001-10-17	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 393–492（100 aa） Fragment：RESIDUES 485-584 Chain F 393–492（100 aa） Fragment：RESIDUES 485-584 Chain G 393–492（100 aa） Fragment：RESIDUES 485-584 Chain H 393–492（100 aa） Fragment：RESIDUES 485-584	Not recorded	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
4DZO Structure of Human Mad1 C-terminal Domain Reveals Its Involvement in Kinetochore Targeting Deposited 2012-03-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 597–718（122 aa） Fragment：C-terminal domain, UNP residues 597-718 Chain B 597–718（122 aa） Fragment：C-terminal domain, UNP residues 597-718	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions hanging-drop vapor diffusion；pH 6.2；293 K；20 mM Tris, 100 mM KCl, 1 mM TCEP, 26% (w/v) PEG1500, 0.1 M Na Cacodylate, pH 6.2, 1mM reduced L-Glutathione;, hanging-drop vapor diffusion, temperature 293K	Resolution 1.76 Å R-free 0.197
7B1F Orthorhombic P212121 Structure of Human Mad1 C-terminal Domain in Complex with Phosphorylated Bub1 CD1 Domain Deposited 2020-11-24	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 597–718（122 aa） Chain B 597–718（122 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；20% PEG 4000, 0.1 M Hepes pH 7.5, 10% isopropanol	Resolution 1.75 Å R-free 0.287
7B1J Orthorhombic P21212 Structure of Human Mad1 C-terminal Domain in Complex with Phosphorylated Bub1 CD1 Domain Deposited 2020-11-25	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 597–718（122 aa） Chain B 597–718（122 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；10% Isopropanol, 0.1 M Na HEPES, pH 7.5, 20% PEG 4000	Resolution 2.90 Å R-free 0.296

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	MD1L1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–122； UniProt 597–718 Author chain B； PDBConstruct 1–122； UniProt 597–718 Author chain E； PDBConstruct 1–122； UniProt 597–718 Author chain F； PDBConstruct 1–122； UniProt 597–718

Mitotic checkpoint serine/threonine-protein kinase BUB1

OrganismNot specified

UniProt O43683

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain C； UniProt 455–479 Chain D； UniProt 455–479	Non-standard monomer：Yes (specific site not provided by mmCIF)	Mitotic spindle assembly checkpoint protein MAD1 × 2 （Q9Y6D9）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；8% Isopropanol, 20% PEG 4000, 0.1 M Na HEPES, pH 7.5	Resolution 2.40 Å R-free 0.281
2	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain G； UniProt 455–479 Chain H； UniProt 455–479	Non-standard monomer：Yes (specific site not provided by mmCIF)	Mitotic spindle assembly checkpoint protein MAD1 × 2 （Q9Y6D9）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；8% Isopropanol, 20% PEG 4000, 0.1 M Na HEPES, pH 7.5	Resolution 2.40 Å R-free 0.281

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 7B1H	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2LAH Solution NMR Structure of Mitotic checkpoint serine/threonine-protein kinase BUB1 N-terminal domain from Homo sapiens, Northeast Structural Genomics Consortium Target HR5460A (Methods Development) Deposited 2011-03-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–150（150 aa） Fragment：N-terminal domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.5；298 K；Pressure ambient NMR sample composition 1.164 mM [U-100% 13C; U-100% 15N] HR5460A, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 1.033 mM [U-10% 13C; U-100% 15N] HR5460A, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
4A1G The crystal structure of the human Bub1 TPR domain in complex with the KI motif of Knl1 Deposited 2011-09-15	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–150（150 aa） Fragment：TPR DOMAIN, RESIDUES 1-150	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；1.25-1.3 M NA MALONATE, PH 6.0.	Resolution 2.60 Å R-free 0.244
4A1G The crystal structure of the human Bub1 TPR domain in complex with the KI motif of Knl1 Deposited 2011-09-15	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–150（150 aa） Fragment：TPR DOMAIN, RESIDUES 1-150	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；1.25-1.3 M NA MALONATE, PH 6.0.	Resolution 2.60 Å R-free 0.244
4A1G The crystal structure of the human Bub1 TPR domain in complex with the KI motif of Knl1 Deposited 2011-09-15	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–150（150 aa） Fragment：TPR DOMAIN, RESIDUES 1-150	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；1.25-1.3 M NA MALONATE, PH 6.0.	Resolution 2.60 Å R-free 0.244
4A1G The crystal structure of the human Bub1 TPR domain in complex with the KI motif of Knl1 Deposited 2011-09-15	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–150（150 aa） Fragment：TPR DOMAIN, RESIDUES 1-150	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；1.25-1.3 M NA MALONATE, PH 6.0.	Resolution 2.60 Å R-free 0.244
4QPM Structure of Bub1 kinase domain Deposited 2014-06-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 749–1094（346 aa） Fragment：UNP residues 749-1094	Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 2 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；293 K；20% PEG3350, 1% Tryptone, 10 mM DTT, 0.1 M HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.20 Å R-free 0.269
4QPM Structure of Bub1 kinase domain Deposited 2014-06-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 749–1094（346 aa） Fragment：UNP residues 749-1094	Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 2 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；293 K；20% PEG3350, 1% Tryptone, 10 mM DTT, 0.1 M HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.20 Å R-free 0.269
4R8Q Structure and substrate recruitment of the human spindle checkpoint kinase bub1 Deposited 2014-09-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 724–1085（362 aa） Fragment：Kinase domain, unp residues 724-1085	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.29；293 K；TO 15 MG/ML BUB1, ATP WAS ADDED TO A FINAL CONCENTRATION OF 10 MM. SITTING DROPS WERE MADE BY MIXING 1.5 MICROLITERS PROTEIN WITH 1.5 MICROLITERS CRYSTALLIZATION SOLUTION (20% W/V PEG 3350, 0.1 M SODIUM FORMATE PH 6.29, 25 MM DTT) AND EQUILIBRATING AGAINST 200 MICROLITERS OF RESERVOIR SOLUTION. LARGE SINGLE CRYSTALS WERE OBTAINED BY REPEATED SEEDING. THE CRYSTALS WERE CRYO-PROTECTED IN RESERVOIR SOLUTION SUPPLEMENTED WITH 18% V/V GLYCEROL AND THEN FLASH-COOLED IN LIQUID PROPANE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K, vapor diffusion, sitting drop	Resolution 2.31 Å R-free 0.264
5DMZ Structure of human Bub1 kinase domain phosphorylated at Ser969 Deposited 2015-09-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 726–1085（360 aa） Fragment：UNP residues 726-1085	Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.6；277 K；0.2 M NaCl, 15% PEG 3350	Resolution 2.40 Å R-free 0.245
5DMZ Structure of human Bub1 kinase domain phosphorylated at Ser969 Deposited 2015-09-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 726–1085（360 aa） Fragment：UNP residues 726-1085	Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.6；277 K；0.2 M NaCl, 15% PEG 3350	Resolution 2.40 Å R-free 0.245
6F7B Crystal structure of the human Bub1 kinase domain in complex with BAY 1816032 Deposited 2017-12-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 726–1085（360 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	CVQ 2-[3,5-bis(fluoranyl)-4-[[3-[5-methoxy-4-[(3-methoxypyridin-4-yl)amino]pyrimidin-2-yl]indazol-1-yl]methyl]phenoxy]ethanol × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.26；277 K；200mM MgCl2, 100mM Tris-HCl pH 7.26, 5% glycerol, 20% PEG 3350	Resolution 2.00 Å R-free 0.254
7B1F Orthorhombic P212121 Structure of Human Mad1 C-terminal Domain in Complex with Phosphorylated Bub1 CD1 Domain Deposited 2020-11-24	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 455–479（25 aa） Chain D 455–479（25 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) 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, SITTING DROP；293 K；20% PEG 4000, 0.1 M Hepes pH 7.5, 10% isopropanol	Resolution 1.75 Å R-free 0.287
7B1J Orthorhombic P21212 Structure of Human Mad1 C-terminal Domain in Complex with Phosphorylated Bub1 CD1 Domain Deposited 2020-11-25	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 455–479（25 aa） Chain D 455–479（25 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) 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, SITTING DROP；293 K；10% Isopropanol, 0.1 M Na HEPES, pH 7.5, 20% PEG 4000	Resolution 2.90 Å R-free 0.296

8 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	BUB1_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–25； UniProt 455–479 Author chain D； PDBConstruct 1–25； UniProt 455–479 Author chain G； PDBConstruct 1–25； UniProt 455–479 Author chain H； PDBConstruct 1–25； UniProt 455–479

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	7b1h
Deposition date deposition_date	2020-11-24
Structure title title	Monoclinic P21 Structure of Human Mad1 C-terminal Domain in Complex with Phosphorylated Bub1 CD1 Domain
Keywords keywords	Mad1, Bub1, spindle assembly checkpoint, mitotic checkpoint complex, CELL CYCLE; CELL CYCLE
Experimental Method method	X-RAY DIFFRACTION

▼

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

Radius of gyration Rg (Guinier) rg_guinier	31.26 Å
Radius of gyration Rg (electron density) rg_electron	30.74 Å
Forward intensity I(0) i0	67223200.00
Molecular weight molecular_weight	64523.0 kDa
Excluded volume excluded_volume	80986 Å³
Envelope volume envelope_volume	108120 Å³
Hydration-shell volume shell_volume	30820 Å³
Envelope diameter envelope_diameter	120.4 Å
Shell Rg shell_rg	35.58 Å
Envelope Rg envelope_rg	31.05 Å
Shape Rg shape_rg	30.69 Å
Total Rg total_rg	31.38 Å
Total atoms total_atoms	4530
Residues n_residues	561
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

▼

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

Maximum dimension Dmax dmax	113.7 Å
Rg (real space) rg_real	31.33 Å
Rg uncertainty (real space) rg_real_error	1.23 Å
I(0) (real space) i0_real	6.7220e+07
I(0) uncertainty (real space) i0_real_error	1.1540e+06
Rg (reciprocal space) rg_reciprocal	31.31 Å
I(0) (reciprocal space) i0_reciprocal	67220000.0000
Solution quality estimate total_estimate	0.8314
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	29.0 Å
Skewness Skewness skewness	0.340
Kurtosis Kurtosis kurtosis	-0.399
Angular range angular_range	— – 0.2550 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	19300000.0000
Real-space data points n_real_points	52
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.728; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.706; Smooth: 0.914

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Mitotic spindle assembly checkpoint protein MAD1
Molecular weight formula_weight	13961.8 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,A,E,F
Atom count atom_count	4542

SSKEVAELKKQVESAELKNQRLKEVFQTKIQEFRKACYTLTGYQIDITTENQYRLTSLYAEHPGDCLIFKATSPSGSKMQLLETEFSHTVGELIEVHLRRQDSIPAFLSSLTLELFSRQTVA

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	Human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Mitotic checkpoint serine/threonine-protein kinase BUB1
Molecular weight formula_weight	3023.3 kDa
EC 编号 ec_number	2.7.11.1
Source method src_method	syn
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,D,G,H

KVQPSPTVHTKEALGFIMNMFQAPTS

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	12

▶

8. Citations (1)

▶

Unit-cell length a length_a	34.630 Å
Unit-cell length b length_b	132.340 Å
Unit-cell length c length_c	82.750 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	93.34 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.400 Å
Low-resolution limit resolution_low	39.430 Å
R factor r_factor	0.2337
R_work r_work	0.2314
R_free r_free	0.2806

fit	/app/data/saxs_computation/b1/7b1h/7b1h.fit
pddf	/app/data/pr_computation/b1/7b1h/7b1h.pr.out
profile	/app/data/saxs_computation/b1/7b1h/7b1h.dat

Monoclinic P21 Structure of Human Mad1 C-terminal Domain in Complex with Phosphorylated Bub1 CD1 Domain

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

Mitotic spindle assembly checkpoint protein MAD1

State in the Current Structure

Other States of the Same Protein in the Database

Mitotic checkpoint serine/threonine-protein kinase BUB1

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

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

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)