SAXSdb — 5b6b

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

MOB kinase activator 1B

Mus musculus

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 1–216 Chain B； UniProt 1–216	Mutation：T35D, T22D	Serine/threonine-protein kinase LATS1 × 2 （Q8BYR2） CL CHLORIDE ION × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；277 K；PEG 3350, sodium sulfate	Resolution 3.54 Å R-free 0.266
2	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain D； UniProt 1–216 Chain K； UniProt 1–216	Mutation：T35D, T22D	Serine/threonine-protein kinase LATS1 × 2 （Q8BYR2） CL CHLORIDE ION × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；277 K；PEG 3350, sodium sulfate	Resolution 3.54 Å R-free 0.266
3	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain F； UniProt 1–216 Chain H； UniProt 1–216	Mutation：T35D, T22D	Serine/threonine-protein kinase LATS1 × 2 （Q8BYR2） CL CHLORIDE ION × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；277 K；PEG 3350, sodium sulfate	Resolution 3.54 Å R-free 0.266
4	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain M； UniProt 1–216 Chain O； UniProt 1–216	Mutation：T35D, T22D	Serine/threonine-protein kinase LATS1 × 2 （Q8BYR2） CL CHLORIDE ION × 1 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；277 K；PEG 3350, sodium sulfate	Resolution 3.54 Å R-free 0.266

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 5B6B	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
5B5V Structure of full-length MOB1b Deposited 2016-05-24	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–216（216 aa） Chain C 1–216（216 aa） Chain E 1–216（216 aa） Chain F 1–216（216 aa）	Not recorded	ZN ZINC ION × 2 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；PEG 3350, Ammonium fluoride	Resolution 2.19 Å R-free 0.246
5B5V Structure of full-length MOB1b Deposited 2016-05-24	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 1–216（216 aa） Chain D 1–216（216 aa）	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；PEG 3350, Ammonium fluoride	Resolution 2.19 Å R-free 0.246
5B5W Crystal structure of MOB1-LATS1 NTR domain complex Deposited 2016-05-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 33–216（184 aa） Fragment：UNP residues 33-216	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；PEG 4000	Resolution 2.96 Å R-free 0.270

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	MOB1B_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–218； UniProt 1–216 Author chain B； PDBConstruct 3–218； UniProt 1–216 Author chain D； PDBConstruct 3–218； UniProt 1–216 Author chain F； PDBConstruct 3–218； UniProt 1–216 Author chain H； PDBConstruct 3–218； UniProt 1–216 Author chain K； PDBConstruct 3–218； UniProt 1–216 Author chain M； PDBConstruct 3–218； UniProt 1–216 Author chain O； PDBConstruct 3–218； UniProt 1–216

Serine/threonine-protein kinase LATS1

Mus musculus

UniProt Q8BYR2

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 621–703 Chain J； UniProt 621–703	Fragment：UNP residues 621-703	MOB kinase activator 1B × 2 （Q8BPB0） CL CHLORIDE ION × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；277 K；PEG 3350, sodium sulfate	Resolution 3.54 Å R-free 0.266
2	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain E； UniProt 621–703 Chain L； UniProt 621–703	Fragment：UNP residues 621-703	MOB kinase activator 1B × 2 （Q8BPB0） CL CHLORIDE ION × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；277 K；PEG 3350, sodium sulfate	Resolution 3.54 Å R-free 0.266
3	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain G； UniProt 621–703 Chain I； UniProt 621–703	Fragment：UNP residues 621-703	MOB kinase activator 1B × 2 （Q8BPB0） CL CHLORIDE ION × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；277 K；PEG 3350, sodium sulfate	Resolution 3.54 Å R-free 0.266
4	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain N； UniProt 621–703 Chain P； UniProt 621–703	Fragment：UNP residues 621-703	MOB kinase activator 1B × 2 （Q8BPB0） CL CHLORIDE ION × 1 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；277 K；PEG 3350, sodium sulfate	Resolution 3.54 Å R-free 0.266

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 5B6B	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6J68 Structure of KIBRA and LATS1 Complex Deposited 2019-01-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 545–568（24 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8；289 K；0.1M Tris, 28% PEG 4000	Resolution 2.50 Å R-free 0.274
6J68 Structure of KIBRA and LATS1 Complex Deposited 2019-01-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 545–568（24 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8；289 K；0.1M Tris, 28% PEG 4000	Resolution 2.50 Å R-free 0.274

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	LATS1_MOUSE
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 3–85； UniProt 621–703 Author chain E； PDBConstruct 3–85； UniProt 621–703 Author chain G； PDBConstruct 3–85； UniProt 621–703 Author chain I； PDBConstruct 3–85； UniProt 621–703 Author chain J； PDBConstruct 3–85； UniProt 621–703 Author chain L； PDBConstruct 3–85； UniProt 621–703 Author chain N； PDBConstruct 3–85； UniProt 621–703 Author chain P； PDBConstruct 3–85； UniProt 621–703

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	5b6b
Deposition date deposition_date	2016-05-26
Structure title title	Complex of LATS1 and phosphomimetic MOB1b
Keywords keywords	MOB1 LATS1 Hippo pathway, METAL BINDING PROTEIN-SIGNALING PROTEIN complex; METAL BINDING PROTEIN/SIGNALING PROTEIN
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	52.19 Å
Radius of gyration Rg (electron density) rg_electron	52.57 Å
Forward intensity I(0) i0	808726000.00
Molecular weight molecular_weight	236940.0 kDa
Excluded volume excluded_volume	296950 Å³
Envelope volume envelope_volume	448620 Å³
Hydration-shell volume shell_volume	76603 Å³
Envelope diameter envelope_diameter	190.6 Å
Shell Rg shell_rg	50.02 Å
Envelope Rg envelope_rg	52.06 Å
Shape Rg shape_rg	52.58 Å
Total Rg total_rg	52.45 Å
Total atoms total_atoms	16626
Residues n_residues	1999
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	179.9 Å
Rg (real space) rg_real	52.43 Å
Rg uncertainty (real space) rg_real_error	2.40 Å
I(0) (real space) i0_real	8.0870e+08
I(0) uncertainty (real space) i0_real_error	1.8070e+07
Rg (reciprocal space) rg_reciprocal	51.98 Å
I(0) (reciprocal space) i0_reciprocal	808200000.0000
Solution quality estimate total_estimate	0.8489
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	60.0 Å
Skewness Skewness skewness	0.513
Kurtosis Kurtosis kurtosis	-0.064
Angular range angular_range	— – 0.1500 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	38910000.0000
Real-space data points n_real_points	31
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.830; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.547

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	MOB kinase activator 1B
Molecular weight formula_weight	25305.0 kDa
Mutation mutation	T35D, T22D
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,D,F,H,K,M,O
Atom count atom_count	16626

GPMSFLFGSRSSKDFKPKKNIPEGSHQYELLKHAEADLGSGNLRMAVMLPEGEDLNEWVAVNTVDFFNQINMLYGTITDFCTEESCPVMSAGPKYEYHWADGTNIKKPIKCSAPKYIDYLMTWVQDQLDDETLFPSKIGVPFPKNFMSVAKTILKRLFRVYAHIYHQHFDPVIQLQEEAHLNTSFKHFIFFVQEFNLIDRRELAPLQELIEKLTSKDR

来源 Source

来源生物 organism	Mus musculus
通用名 common_name	Mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Serine/threonine-protein kinase LATS1
Molecular weight formula_weight	10379.0 kDa
EC 编号 ec_number	2.7.11.1
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	J,C,E,G,I,L,N,P

GPKDEERRESRIQSYSPQAFKFFMEQHVENVLKSHQQRLHRKKQLENEMMRVGLSQDAQDQMRKMLCQKESNYIRLKRAKMDKSM

来源 Source

来源生物 organism	Mus musculus
通用名 common_name	Mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	7

Entity 4 Entity 4 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	8

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7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id	5b6bA00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily	30 — MOB kinase activator

Domain ID domain_id	5b6bB00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily	30 — MOB kinase activator

Domain ID domain_id	5b6bD00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily	30 — MOB kinase activator

Domain ID domain_id	5b6bF00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily	30 — MOB kinase activator

Domain ID domain_id	5b6bH00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily	30 — MOB kinase activator

Domain ID domain_id	5b6bK00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily	30 — MOB kinase activator

Domain ID domain_id	5b6bM00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily	30 — MOB kinase activator

Domain ID domain_id	5b6bO00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily	30 — MOB kinase activator

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8. Citations (1)

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Unit-cell length a length_a	168.646 Å
Unit-cell length b length_b	301.437 Å
Unit-cell length c length_c	127.379 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	64

Space group space_group	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	3.536 Å
Low-resolution limit resolution_low	48.644 Å
R factor r_factor	0.2245
R_work r_work	0.2223
R_free r_free	0.2656

fit	/app/data/saxs_computation/b6/5b6b/5b6b.fit
pddf	/app/data/pr_computation/b6/5b6b/5b6b.pr.out
profile	/app/data/saxs_computation/b6/5b6b/5b6b.dat

Complex of LATS1 and phosphomimetic MOB1b

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

MOB kinase activator 1B

State in the Current Structure

Other States of the Same Protein in the Database

Serine/threonine-protein kinase LATS1

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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)