SAXSdb — 5brm

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

MOB kinase activator 1A

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 × 15 PDB declaration: pentadecameric（15） Consistent with protein copy count	Chain A； UniProt 41–216 Chain B； UniProt 41–216 Chain C； UniProt 41–216 Chain D； UniProt 41–216 Chain E； UniProt 41–216 Chain F； UniProt 41–216	Fragment：UNP residues 41-216	Serine/threonine-protein kinase 3 × 9 （Q13188） ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；2.4 M Na Malonate	Resolution 2.65 Å R-free 0.268

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 5BRM	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1PI1 Crystal structure of a human Mob1 protein; toward understanding Mob-regulated cell cycle pathways. Deposited 2003-05-29	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 33–216（184 aa） Fragment：sequence database residues 33-216	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；298 K；Sodium Citrate, Bis-Tris Propane, isopropanol, DTT, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.00 Å R-free 0.242
4J1V Functional and structural studies of MOBKL1B, a Salvador/Warts/Hippo tumor suppressor pathway, in HCV replication Deposited 2013-02-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 33–216（184 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；279 K；0.1 M HEPES, 0.1 M KCl, 15% PEG5000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.95 Å R-free 0.225
4J1V Functional and structural studies of MOBKL1B, a Salvador/Warts/Hippo tumor suppressor pathway, in HCV replication Deposited 2013-02-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 33–216（184 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；279 K；0.1 M HEPES, 0.1 M KCl, 15% PEG5000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.95 Å R-free 0.225
4JIZ Human Mob1-phosphopeptide complex Deposited 2013-03-07	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 40–211（172 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.10 Å R-free 0.226
5BRK pMob1-Lats1 complex Deposited 2015-05-31	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 1–216（216 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；293 K；0.2 M di-Ammonium citrate 20% (W/V) PEG 3,350	Resolution 2.30 Å R-free 0.221
5TWF Regulation of protein interactions by MOB1 phosphorylation Deposited 2016-11-13	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 1–216（216 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；298 K；0.1 M MES pH 5.5, 0.2 M NH4Cl, and 20% PEG 6000	Resolution 3.14 Å R-free 0.291
5TWF Regulation of protein interactions by MOB1 phosphorylation Deposited 2016-11-13	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 1–216（216 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；298 K；0.1 M MES pH 5.5, 0.2 M NH4Cl, and 20% PEG 6000	Resolution 3.14 Å R-free 0.291
5TWF Regulation of protein interactions by MOB1 phosphorylation Deposited 2016-11-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–216（216 aa）	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；298 K；0.1 M MES pH 5.5, 0.2 M NH4Cl, and 20% PEG 6000	Resolution 3.14 Å R-free 0.291
5TWF Regulation of protein interactions by MOB1 phosphorylation Deposited 2016-11-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 1–216（216 aa）	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；298 K；0.1 M MES pH 5.5, 0.2 M NH4Cl, and 20% PEG 6000	Resolution 3.14 Å R-free 0.291
5TWG human MOB1A bound to human MST1 phosphorylated T353 peptide Deposited 2016-11-13	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 1–216（216 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；298 K；0.1 M MES pH 6.0, 0.2 M LiCl and 20% PEG 6000	Resolution 2.30 Å R-free 0.252
5TWH human MOB1A bound to MST1 phosphorylated T367 peptide Deposited 2016-11-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–216（216 aa）	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；298 K；0.1 M MES pH 6.0, 0.2 M LiCl and 20% PEG 6000	Resolution 2.50 Å R-free 0.260
5XQZ Structure of the MOB1-NDR2 complex Deposited 2017-06-07	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 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；287 K；PEG 3350, HEPES, magnesium chloride	Resolution 2.10 Å R-free 0.244
5XQZ Structure of the MOB1-NDR2 complex Deposited 2017-06-07	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 B 33–216（184 aa） Fragment：UNP RESIDUES 33-216	Not recorded	ZN ZINC ION × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；287 K；PEG 3350, HEPES, magnesium chloride	Resolution 2.10 Å R-free 0.244
6MCP L. pneumophila effector kinase LegK7 (AMP-PNP bound) in complex with human MOB1A Deposited 2018-09-01	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 B 33–213（181 aa） Fragment：UNP residues 33-213	Not recorded	PG4 TETRAETHYLENE GLYCOL × 2 PEG DI(HYDROXYETHYL)ETHER × 9 P6G HEXAETHYLENE GLYCOL × 3 ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；288 K；0.1 M HEPES, pH 7.5, 21% PEG600, 0.2 M sodium chloride, 20 mM succinate	Resolution 2.50 Å R-free 0.233
6MCP L. pneumophila effector kinase LegK7 (AMP-PNP bound) in complex with human MOB1A Deposited 2018-09-01	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 33–213（181 aa） Fragment：UNP residues 33-213	Not recorded	PG4 TETRAETHYLENE GLYCOL × 1 PEG DI(HYDROXYETHYL)ETHER × 9 P6G HEXAETHYLENE GLYCOL × 1 ZN ZINC ION × 1 MN MANGANESE (II) ION × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；288 K；0.1 M HEPES, pH 7.5, 21% PEG600, 0.2 M sodium chloride, 20 mM succinate	Resolution 2.50 Å R-free 0.233
6MCQ L. pneumophila effector kinase LegK7 in complex with human MOB1A Deposited 2018-09-01	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 B 33–216（184 aa） Fragment：UNP residues 33-216	Not recorded	PEG DI(HYDROXYETHYL)ETHER × 10 P6G HEXAETHYLENE GLYCOL × 3 PG4 TETRAETHYLENE GLYCOL × 3 ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；288 K；0.1 M HEPES, pH 7.5, 23% PEG600, 0.1 M lithium chloride, 20 mM succinate, pH 7.0	Resolution 2.57 Å R-free 0.245
6MCQ L. pneumophila effector kinase LegK7 in complex with human MOB1A Deposited 2018-09-01	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 33–216（184 aa） Fragment：UNP residues 33-216	Not recorded	PEG DI(HYDROXYETHYL)ETHER × 6 PG4 TETRAETHYLENE GLYCOL × 2 ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；288 K；0.1 M HEPES, pH 7.5, 23% PEG600, 0.1 M lithium chloride, 20 mM succinate, pH 7.0	Resolution 2.57 Å R-free 0.245

10 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	MOB1A_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–177； UniProt 41–216 Author chain B； PDBConstruct 2–177； UniProt 41–216 Author chain C； PDBConstruct 2–177； UniProt 41–216 Author chain D； PDBConstruct 2–177； UniProt 41–216 Author chain E； PDBConstruct 2–177； UniProt 41–216 Author chain F； PDBConstruct 2–177； UniProt 41–216

Serine/threonine-protein kinase 3

OrganismNot specified

UniProt Q13188

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 × 15 PDB declaration: pentadecameric（15） Consistent with protein copy count	Chain G； UniProt 371–401 Chain H； UniProt 371–401 Chain I； UniProt 371–401 Chain J； UniProt 371–401 Chain K； UniProt 371–401 Chain L； UniProt 371–401 Chain M； UniProt 371–401 Chain N； UniProt 371–401 Chain O； UniProt 371–401	Fragment：UNP residues 371-401 Non-standard monomer：Yes (specific site not provided by mmCIF)	MOB kinase activator 1A × 6 （Q9H8S9） ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；2.4 M Na Malonate	Resolution 2.65 Å R-free 0.268

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 5BRM	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3WWS Crystal structure of Serine/threonine-protein kinase 3 Deposited 2014-06-27	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 436–484（49 aa） Fragment：UNP residues 436-484 Chain B 436–484（49 aa） Fragment：UNP residues 436-484	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, HANGING DROP；pH 7.4；293 K；0.1M Tris-HCl pH 7.4. 10%(m/v) PEG3350, 0.1M (NH4)3PO4, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.01 Å R-free 0.311
3WWS Crystal structure of Serine/threonine-protein kinase 3 Deposited 2014-06-27	Different construct 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 C 436–484（49 aa） Fragment：UNP residues 436-484 Chain D 436–484（49 aa） Fragment：UNP residues 436-484	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, HANGING DROP；pH 7.4；293 K；0.1M Tris-HCl pH 7.4. 10%(m/v) PEG3350, 0.1M (NH4)3PO4, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.01 Å R-free 0.311
4HKD Crystal structure of human MST2 SARAH domain Deposited 2012-10-15	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 436–484（49 aa） Fragment：SARAH DOMAIN, UNP residues 436-484 Chain B 436–484（49 aa） Fragment：SARAH DOMAIN, UNP residues 436-484	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, HANGING DROP；pH 4.6；289 K；0.4M calcium chloride dihydrate, 0.1M sodium acetate trihydrate, 5%(v/v) 2-propanol, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 1.50 Å R-free 0.231
4HKD Crystal structure of human MST2 SARAH domain Deposited 2012-10-15	Different construct 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 C 436–484（49 aa） Fragment：SARAH DOMAIN, UNP residues 436-484 Chain D 436–484（49 aa） Fragment：SARAH DOMAIN, UNP residues 436-484	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, HANGING DROP；pH 4.6；289 K；0.4M calcium chloride dihydrate, 0.1M sodium acetate trihydrate, 5%(v/v) 2-propanol, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 1.50 Å R-free 0.231
4L0N Crystal structure of STK3 (MST2) SARAH domain Deposited 2013-05-31	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 436–484（49 aa） Fragment：SARAH domain (UNP residues 436-484) Chain B 436–484（49 aa） Fragment：SARAH domain (UNP residues 436-484)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.9；277.15 K；30% MPD, 0.1M acetate pH 4.9, 0.2M calcium chloride, VAPOR DIFFUSION, SITTING DROP, temperature 277.15K	Resolution 1.40 Å R-free 0.207
4L0N Crystal structure of STK3 (MST2) SARAH domain Deposited 2013-05-31	Different construct 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 C 436–484（49 aa） Fragment：SARAH domain (UNP residues 436-484) Chain D 436–484（49 aa） Fragment：SARAH domain (UNP residues 436-484)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.9；277.15 K；30% MPD, 0.1M acetate pH 4.9, 0.2M calcium chloride, VAPOR DIFFUSION, SITTING DROP, temperature 277.15K	Resolution 1.40 Å R-free 0.207
4L0N Crystal structure of STK3 (MST2) SARAH domain Deposited 2013-05-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain E 436–484（49 aa） Fragment：SARAH domain (UNP residues 436-484) Chain F 436–484（49 aa） Fragment：SARAH domain (UNP residues 436-484)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.9；277.15 K；30% MPD, 0.1M acetate pH 4.9, 0.2M calcium chloride, VAPOR DIFFUSION, SITTING DROP, temperature 277.15K	Resolution 1.40 Å R-free 0.207
4L0N Crystal structure of STK3 (MST2) SARAH domain Deposited 2013-05-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain G 436–484（49 aa） Fragment：SARAH domain (UNP residues 436-484) Chain H 436–484（49 aa） Fragment：SARAH domain (UNP residues 436-484)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.9；277.15 K；30% MPD, 0.1M acetate pH 4.9, 0.2M calcium chloride, VAPOR DIFFUSION, SITTING DROP, temperature 277.15K	Resolution 1.40 Å R-free 0.207
4L0N Crystal structure of STK3 (MST2) SARAH domain Deposited 2013-05-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain I 436–484（49 aa） Fragment：SARAH domain (UNP residues 436-484)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.9；277.15 K；30% MPD, 0.1M acetate pH 4.9, 0.2M calcium chloride, VAPOR DIFFUSION, SITTING DROP, temperature 277.15K	Resolution 1.40 Å R-free 0.207
4L0N Crystal structure of STK3 (MST2) SARAH domain Deposited 2013-05-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain J 436–484（49 aa） Fragment：SARAH domain (UNP residues 436-484)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.9；277.15 K；30% MPD, 0.1M acetate pH 4.9, 0.2M calcium chloride, VAPOR DIFFUSION, SITTING DROP, temperature 277.15K	Resolution 1.40 Å R-free 0.207
4LG4 Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5 Deposited 2013-06-27	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 16–313（298 aa） Fragment：kinase domain, UNP residues 16-313	Mutation：D146N	GOL GLYCEROL × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.7；277 K；0.2 M sodium citrate, 15% (w/v) PEG 3350, 0.1 M HEPES, pH 7.7, vapor diffusion, hanging drop, temperature 277K	Resolution 2.42 Å R-free 0.231
4LG4 Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5 Deposited 2013-06-27	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 16–313（298 aa） Fragment：kinase domain, UNP residues 16-313	Mutation：D146N	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.7；277 K；0.2 M sodium citrate, 15% (w/v) PEG 3350, 0.1 M HEPES, pH 7.7, vapor diffusion, hanging drop, temperature 277K	Resolution 2.42 Å R-free 0.231
4LG4 Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5 Deposited 2013-06-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 16–313（298 aa） Fragment：kinase domain, UNP residues 16-313	Mutation：D146N	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.7；277 K；0.2 M sodium citrate, 15% (w/v) PEG 3350, 0.1 M HEPES, pH 7.7, vapor diffusion, hanging drop, temperature 277K	Resolution 2.42 Å R-free 0.231
4LG4 Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5 Deposited 2013-06-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 16–313（298 aa） Fragment：kinase domain, UNP residues 16-313	Mutation：D146N	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.7；277 K；0.2 M sodium citrate, 15% (w/v) PEG 3350, 0.1 M HEPES, pH 7.7, vapor diffusion, hanging drop, temperature 277K	Resolution 2.42 Å R-free 0.231
4LG4 Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5 Deposited 2013-06-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain E 16–313（298 aa） Fragment：kinase domain, UNP residues 16-313	Mutation：D146N	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.7；277 K；0.2 M sodium citrate, 15% (w/v) PEG 3350, 0.1 M HEPES, pH 7.7, vapor diffusion, hanging drop, temperature 277K	Resolution 2.42 Å R-free 0.231
4LG4 Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5 Deposited 2013-06-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain F 16–313（298 aa） Fragment：kinase domain, UNP residues 16-313	Mutation：D146N	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.7；277 K；0.2 M sodium citrate, 15% (w/v) PEG 3350, 0.1 M HEPES, pH 7.7, vapor diffusion, hanging drop, temperature 277K	Resolution 2.42 Å R-free 0.231
4LGD Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5 Deposited 2013-06-27	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 9–313（305 aa） Fragment：kinase domain, SARAH domain, UNP residues 1-313, 428-491 Chain A 428–491（64 aa） Fragment：kinase domain, SARAH domain, UNP residues 1-313, 428-491	Mutation：D146N Mutation：D146N	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.1 M Bis-Tris propane, 200 mM Na2SO4, 20% (w/v) PEG 3350, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.05 Å R-free 0.244
4LGD Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5 Deposited 2013-06-27	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 C 9–313（305 aa） Fragment：kinase domain, SARAH domain, UNP residues 1-313, 428-491 Chain C 428–491（64 aa） Fragment：kinase domain, SARAH domain, UNP residues 1-313, 428-491	Mutation：D146N Mutation：D146N	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 SO4 SULFATE ION × 1 NA SODIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.1 M Bis-Tris propane, 200 mM Na2SO4, 20% (w/v) PEG 3350, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.05 Å R-free 0.244
4LGD Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5 Deposited 2013-06-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 9–313（305 aa） Fragment：kinase domain, SARAH domain, UNP residues 1-313, 428-491 Chain D 428–491（64 aa） Fragment：kinase domain, SARAH domain, UNP residues 1-313, 428-491	Mutation：D146N Mutation：D146N	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 SO4 SULFATE ION × 3 NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.1 M Bis-Tris propane, 200 mM Na2SO4, 20% (w/v) PEG 3350, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.05 Å R-free 0.244
4LGD Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5 Deposited 2013-06-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 9–313（305 aa） Fragment：kinase domain, SARAH domain, UNP residues 1-313, 428-491 Chain B 428–491（64 aa） Fragment：kinase domain, SARAH domain, UNP residues 1-313, 428-491	Mutation：D146N Mutation：D146N	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.1 M Bis-Tris propane, 200 mM Na2SO4, 20% (w/v) PEG 3350, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.05 Å R-free 0.244
4LGD Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5 Deposited 2013-06-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 9–313（305 aa） Fragment：kinase domain, SARAH domain, UNP residues 1-313, 428-491 Chain A 428–491（64 aa） Fragment：kinase domain, SARAH domain, UNP residues 1-313, 428-491 Chain B 9–313（305 aa） Fragment：kinase domain, SARAH domain, UNP residues 1-313, 428-491 Chain B 428–491（64 aa） Fragment：kinase domain, SARAH domain, UNP residues 1-313, 428-491	Mutation：D146N Mutation：D146N Mutation：D146N Mutation：D146N	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 SO4 SULFATE ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.1 M Bis-Tris propane, 200 mM Na2SO4, 20% (w/v) PEG 3350, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.05 Å R-free 0.244
4LGD Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5 Deposited 2013-06-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 9–313（305 aa） Fragment：kinase domain, SARAH domain, UNP residues 1-313, 428-491 Chain C 428–491（64 aa） Fragment：kinase domain, SARAH domain, UNP residues 1-313, 428-491 Chain D 9–313（305 aa） Fragment：kinase domain, SARAH domain, UNP residues 1-313, 428-491 Chain D 428–491（64 aa） Fragment：kinase domain, SARAH domain, UNP residues 1-313, 428-491	Mutation：D146N Mutation：D146N Mutation：D146N Mutation：D146N	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 SO4 SULFATE ION × 4 NA SODIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.1 M Bis-Tris propane, 200 mM Na2SO4, 20% (w/v) PEG 3350, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.05 Å R-free 0.244
4OH9 Crystal Structure of the human MST2 SARAH homodimer Deposited 2014-01-17	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 436–484（49 aa） Fragment：SARAH domain Chain B 436–484（49 aa） Fragment：SARAH domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；2.0 M NaCl, 8% polyethylene glycol (PEG) 6000, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.70 Å R-free 0.272
5DH3 Crystal structure of MST2 in complex with XMU-MP-1 Deposited 2015-08-29	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 15–313（299 aa） Chain B 15–313（299 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	5BS 4-[(5,10-dimethyl-6-oxo-6,10-dihydro-5H-pyrimido[5,4-b]thieno[3,2-e][1,4]diazepin-2-yl)amino]benzenesulfonamide × 2 CL CHLORIDE ION × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；0.1M Bis-Tris pH 6.5, 28% PEG3350, 0.2M (NH4)2SO4	Resolution 2.47 Å R-free 0.247
6AO5 Crystal structure of human MST2 in complex with SAV1 SARAH domain Deposited 2017-08-15	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 16–313（298 aa） Fragment：kinase domain (UNP residues 16-313, 428-491) Chain A 428–491（64 aa） Fragment：kinase domain (UNP residues 16-313, 428-491)	Mutation：D146N Mutation：D146N	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.05 M NaCl, 0.1 M Hepes, 0.19 mM CYMAL-7, 1 mM TCEP, 40% PEG 400	Resolution 2.96 Å R-free 0.256
8A66 Crystal structure of MST2 in complex with XMU-MP-1 Deposited 2022-06-16	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 16–312（297 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	5BS 4-[(5,10-dimethyl-6-oxo-6,10-dihydro-5H-pyrimido[5,4-b]thieno[3,2-e][1,4]diazepin-2-yl)amino]benzenesulfonamide × 1 NA SODIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2M Ammonium citrate pH 7.0 and 18% PEG3350	Resolution 1.90 Å R-free 0.258
8A66 Crystal structure of MST2 in complex with XMU-MP-1 Deposited 2022-06-16	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 16–312（297 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	5BS 4-[(5,10-dimethyl-6-oxo-6,10-dihydro-5H-pyrimido[5,4-b]thieno[3,2-e][1,4]diazepin-2-yl)amino]benzenesulfonamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2M Ammonium citrate pH 7.0 and 18% PEG3350	Resolution 1.90 Å R-free 0.258

9 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	STK3_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain G； PDBConstruct 1–31； UniProt 371–401 Author chain H； PDBConstruct 1–31； UniProt 371–401 Author chain I； PDBConstruct 1–31； UniProt 371–401 Author chain J； PDBConstruct 1–31； UniProt 371–401 Author chain K； PDBConstruct 1–31； UniProt 371–401 Author chain L； PDBConstruct 1–31； UniProt 371–401 Author chain M； PDBConstruct 1–31； UniProt 371–401 Author chain N； PDBConstruct 1–31； UniProt 371–401 Author chain O； PDBConstruct 1–31； UniProt 371–401

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	5brm
Deposition date deposition_date	2015-05-31
Structure title title	Structural basis for Mob1-dependent activation of the core Mst-Lats kinase cascade in Hippo signaling
Keywords keywords	Mst2, Mob1, Hippo, Transferase-Signaling Protein complex; Transferase/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	35.09 Å
Radius of gyration Rg (electron density) rg_electron	33.98 Å
Forward intensity I(0) i0	236805000.00
Molecular weight molecular_weight	126650.0 kDa
Excluded volume excluded_volume	159190 Å³
Envelope volume envelope_volume	207670 Å³
Hydration-shell volume shell_volume	49200 Å³
Envelope diameter envelope_diameter	112.8 Å
Shell Rg shell_rg	42.46 Å
Envelope Rg envelope_rg	33.23 Å
Shape Rg shape_rg	33.93 Å
Total Rg total_rg	34.78 Å
Total atoms total_atoms	17458
Residues n_residues	1054
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	106.3 Å
Rg (real space) rg_real	34.90 Å
Rg uncertainty (real space) rg_real_error	0.63 Å
I(0) (real space) i0_real	2.3680e+08
I(0) uncertainty (real space) i0_real_error	3.3230e+06
Rg (reciprocal space) rg_reciprocal	35.02 Å
I(0) (reciprocal space) i0_reciprocal	236800000.0000
Solution quality estimate total_estimate	0.9101
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	49.6 Å
Skewness Skewness skewness	0.040
Kurtosis Kurtosis kurtosis	-0.685
Angular range angular_range	— – 0.2250 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	103800000.0000
Real-space data points n_real_points	46
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.960; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.952

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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 1A
Molecular weight formula_weight	20724.8 kDa
Source method src_method	man
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F
Atom count atom_count	17464

GLRQAVMLPEGEDLNEWIAVNTVDFFNQINMLYGTITEFCTEASCPVMSAGPRYEYHWADGTNIKKPIKCSAPKYIDYLMTWVQDQLDDETLFPSKIGVPFPKNFMSVAKTILKRLFRVYAHIYHQHFDSVMQLQEEAHLNTSFKHFIFFVQEFNLIDRRELAPLQELIEKLGSKDR

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	Serine/threonine-protein kinase 3
Molecular weight formula_weight	3778.9 kDa
EC 编号 ec_number	2.7.11.1
Source method src_method	syn
Copy count entity_count	9

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G,H,I,J,K,L,M,N,O

DEEEEDGTMKRNATSPQVQRPSFMDYFDKQD

Entity 3 Entity 3 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	6

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7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id	5brmA00
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	5brmB00
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	5brmC00
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	5brmD00
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	5brmE00
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	5brmF00
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	142.188 Å
Unit-cell length b length_b	142.188 Å
Unit-cell length c length_c	135.981 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	54

Space group space_group	P 31 2 1
Space-group number int_tables_number	152
Crystal system crystal_system	—

Resolution resolution	2.651 Å
Low-resolution limit resolution_low	39.295 Å
R factor r_factor	0.2452
R_work r_work	0.2441
R_free r_free	0.2681

fit	/app/data/saxs_computation/br/5brm/5brm.fit
pddf	/app/data/pr_computation/br/5brm/5brm.pr.out
profile	/app/data/saxs_computation/br/5brm/5brm.dat

Structural basis for Mob1-dependent activation of the core Mst-Lats kinase cascade in Hippo signaling

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

MOB kinase activator 1A

State in the Current Structure

Other States of the Same Protein in the Database

Serine/threonine-protein kinase 3

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

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)