SAXSdb — 4a1g

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

MITOTIC CHECKPOINT SERINE/THREONINE-PROTEIN KINASE BUB1

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–150	Fragment：TPR DOMAIN, RESIDUES 1-150	PROTEIN CASC5 × 1 （Q8NG31）	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
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 1–150	Fragment：TPR DOMAIN, RESIDUES 1-150	PROTEIN CASC5 × 1 （Q8NG31）	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
3	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 1–150	Fragment：TPR DOMAIN, RESIDUES 1-150	PROTEIN CASC5 × 1 （Q8NG31）	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
4	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 1–150	Fragment：TPR DOMAIN, RESIDUES 1-150	PROTEIN CASC5 × 1 （Q8NG31）	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

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 4A1G	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 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
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 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 construct Different mutation/modification Different oligomeric state 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
7B1H Monoclinic P21 Structure of Human Mad1 C-terminal Domain in Complex with Phosphorylated Bub1 CD1 Domain Deposited 2020-11-24	Different construct Different mutation/modification Different oligomeric state 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；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
7B1H Monoclinic P21 Structure of Human Mad1 C-terminal Domain in Complex with Phosphorylated Bub1 CD1 Domain Deposited 2020-11-24	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain G 455–479（25 aa） Chain H 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；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
7B1J Orthorhombic P21212 Structure of Human Mad1 C-terminal Domain in Complex with Phosphorylated Bub1 CD1 Domain Deposited 2020-11-25	Different construct Different mutation/modification Different oligomeric state 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 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	BUB1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–152； UniProt 1–150 Author chain B； PDBConstruct 3–152； UniProt 1–150 Author chain C； PDBConstruct 3–152； UniProt 1–150 Author chain D； PDBConstruct 3–152； UniProt 1–150

PROTEIN CASC5

HOMO SAPIENS

UniProt Q8NG31

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain E； UniProt 150–200	Fragment：KI MOTIF, RESIDUES 150-200	MITOTIC CHECKPOINT SERINE/THREONINE-PROTEIN KINASE BUB1 × 1 （O43683）	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
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain F； UniProt 150–200	Fragment：KI MOTIF, RESIDUES 150-200	MITOTIC CHECKPOINT SERINE/THREONINE-PROTEIN KINASE BUB1 × 1 （O43683）	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
3	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain G； UniProt 150–200	Fragment：KI MOTIF, RESIDUES 150-200	MITOTIC CHECKPOINT SERINE/THREONINE-PROTEIN KINASE BUB1 × 1 （O43683）	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
4	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain H； UniProt 150–200	Fragment：KI MOTIF, RESIDUES 150-200	MITOTIC CHECKPOINT SERINE/THREONINE-PROTEIN KINASE BUB1 × 1 （O43683）	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

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 4A1G	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3SI5 Kinetochore-BUBR1 kinase complex Deposited 2011-06-17	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain X 234–252（19 aa） Fragment：UNP residues 234-252	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；292 K；15% PEG 6000, 0.1M Magnesium Acetate, 0.1M Sodium Cacodylate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.20 Å R-free 0.247
3SI5 Kinetochore-BUBR1 kinase complex Deposited 2011-06-17	Different construct Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain Y 234–252（19 aa） Fragment：UNP residues 234-252	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；292 K；15% PEG 6000, 0.1M Magnesium Acetate, 0.1M Sodium Cacodylate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.20 Å R-free 0.247
4NF9 Structure of the Knl1/Nsl1 complex Deposited 2013-10-31	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 2117–2337（221 aa） Fragment：Knl1 C-terminal domain, UNP residues 2117-2337	Non-standard monomer：Yes (specific site not provided by mmCIF)	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；16-20 % (v/v) PEG 3350, 220 mM sodium citrate and 100 mM MES (pH 6 or 6.5) and 100 mM Hepes (pH 7), VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.80 Å R-free 0.265
4NF9 Structure of the Knl1/Nsl1 complex Deposited 2013-10-31	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 2117–2337（221 aa） Fragment：Knl1 C-terminal domain, UNP residues 2117-2337	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 7；293 K；16-20 % (v/v) PEG 3350, 220 mM sodium citrate and 100 mM MES (pH 6 or 6.5) and 100 mM Hepes (pH 7), VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.80 Å R-free 0.265
4NFA Structure of the C-terminal doamin of Knl1 Deposited 2013-10-31	Different construct 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 2117–2323（207 aa） Fragment：Knl1 C-terminal domain, UNP residues 2131-2337	Not recorded	CL CHLORIDE ION × 1 GOL GLYCEROL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；120-300 KSCN, 100 mM BisTris Propane (pH 8.6-9.2), 17 % (v/v) PEG 3350 and 1 mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.242
8PPR Structure of the human outer kinetochore KMN network complex Deposited 2023-07-08	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain K 1–2342（2342 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
8Q5H Human KMN network (outer kinetochore) Deposited 2023-08-09	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain K 2021–2342（322 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.50 Å

5 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CASC5_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain E； PDBConstruct 3–53； UniProt 150–200 Author chain F； PDBConstruct 3–53； UniProt 150–200 Author chain G； PDBConstruct 3–53； UniProt 150–200 Author chain H； PDBConstruct 3–53； UniProt 150–200

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	4a1g
Deposition date deposition_date	2011-09-15
Structure title title	The crystal structure of the human Bub1 TPR domain in complex with the KI motif of Knl1
Keywords keywords	CELL CYCLE, TRANSFERASE, SPINDLE ASSEMBLY CHECKPOINT, MITOSIS, TPR REPEAT, KNL1, KMN NETWORK; CELL CYCLE
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	27.48 Å
Radius of gyration Rg (electron density) rg_electron	26.26 Å
Forward intensity I(0) i0	90570500.00
Molecular weight molecular_weight	75839.0 kDa
Excluded volume excluded_volume	95158 Å³
Envelope volume envelope_volume	114640 Å³
Hydration-shell volume shell_volume	35603 Å³
Envelope diameter envelope_diameter	90.1 Å
Shell Rg shell_rg	34.37 Å
Envelope Rg envelope_rg	26.13 Å
Shape Rg shape_rg	26.24 Å
Total Rg total_rg	27.17 Å
Total atoms total_atoms	5377
Residues n_residues	650
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

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

Maximum dimension Dmax dmax	85.2 Å
Rg (real space) rg_real	27.33 Å
Rg uncertainty (real space) rg_real_error	0.50 Å
I(0) (real space) i0_real	9.0570e+07
I(0) uncertainty (real space) i0_real_error	1.4100e+06
Rg (reciprocal space) rg_reciprocal	27.38 Å
I(0) (reciprocal space) i0_reciprocal	90570000.0000
Solution quality estimate total_estimate	0.9040
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	35.3 Å
Skewness Skewness skewness	0.186
Kurtosis Kurtosis kurtosis	-0.463
Angular range angular_range	— – 0.2900 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	34380000.0000
Real-space data points n_real_points	59
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.926; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.979

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	MITOTIC CHECKPOINT SERINE/THREONINE-PROTEIN KINASE BUB1
Molecular weight formula_weight	18121.3 kDa
EC 编号 ec_number	2.7.11.1
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	5497

GPMDTPENVLQMLEAHMQSYKGNDPLGEWERYIQWVEENFPENKEYLITLLEHLMKEFLDKKKYHNDPRFISYCLKFAEYNSDLHQFFEFLYNHGIGTLSSPLYIAWAGHLEAQGELQHASAVLQRGIQNQAEPREFLQQQYRLFQTRLTET

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	PROTEIN CASC5
Molecular weight formula_weight	5911.8 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,F,G,H

GPQMDLTSSHTVMITKGLLDNPISEKSTKIDTTSFLANLKLHTEDSRMKKEVN

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 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	120

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7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id	4a1gA00
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily	430 —

Domain ID domain_id	4a1gB00
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily	430 —

Domain ID domain_id	4a1gC00
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily	430 —

Domain ID domain_id	4a1gD00
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily	430 —

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8. Citations (1)

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Unit-cell length a length_a	59.279 Å
Unit-cell length b length_b	130.969 Å
Unit-cell length c length_c	74.956 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	110.17 °
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	2.600 Å
Low-resolution limit resolution_low	61.983 Å
R factor r_factor	0.1889
R_work r_work	0.1859
R_free r_free	0.2436

fit	/app/data/saxs_computation/a1/4a1g/4a1g.fit
pddf	/app/data/pr_computation/a1/4a1g/4a1g.pr.out
profile	/app/data/saxs_computation/a1/4a1g/4a1g.dat

The crystal structure of the human Bub1 TPR domain in complex with the KI motif of Knl1

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

MITOTIC CHECKPOINT SERINE/THREONINE-PROTEIN KINASE BUB1

State in the Current Structure

Other States of the Same Protein in the Database

PROTEIN CASC5

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

来源 Source

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)