9f8t

Clathrin terminal domain complexed with C-terminus of AAK1L

Method: X-RAY DIFFRACTION D_max: 70.3 Å Quality: GOOD

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

Clathrin heavy chain 1

Bos taurus

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain A； UniProt 1–363	Not recorded	AP2-associated protein kinase 1 × 2 （Q2M2I8）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6；293.15 K；20% PEG 3,350; 100 mM Bis-Tris propane, pH 6.0; 200 mM sodium citrate; 10 mM DTT	Resolution 1.71 Å R-free 0.209

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 9F8T	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1B89 CLATHRIN HEAVY CHAIN PROXIMAL LEG SEGMENT (BOVINE) Deposited 1999-05-27	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1074–1522（449 aa） Fragment：PROXIMAL LEG	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；250 MM SODIUM FORMATE, 100 MM TRIS-HCL, PH 8, pH 8.0	Resolution 2.60 Å R-free 0.279
1UTC Clathrin terminal domain complexed with TLPWDLWTT Deposited 2003-12-08	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–363（363 aa） Fragment：TERMINAL DOMAIN, RESIDUES 1-363	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；VAPOUR DIFFUSION OVER A RESERVOIR CONTAINING 20% PEG8000, 200 MM MGCL2, 4 MM DTT,100 MM CAPS PH 9, DRIED UP DROP	Resolution 2.30 Å R-free 0.253
1UTC Clathrin terminal domain complexed with TLPWDLWTT Deposited 2003-12-08	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–363（363 aa） Fragment：TERMINAL DOMAIN, RESIDUES 1-363	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；VAPOUR DIFFUSION OVER A RESERVOIR CONTAINING 20% PEG8000, 200 MM MGCL2, 4 MM DTT,100 MM CAPS PH 9, DRIED UP DROP	Resolution 2.30 Å R-free 0.253
1XI4 Clathrin D6 Coat Deposited 2004-09-21	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 216 PDB declaration: 216-MERIC	Chain A 1–1630（1630 aa） Fragment：residues 1-1630 Chain B 1–1630（1630 aa） Fragment：residues 1-1630 Chain C 1–1630（1630 aa） Fragment：residues 1-1630 Chain D 1–1630（1630 aa） Fragment：residues 1-1630 Chain E 1–1630（1630 aa） Fragment：residues 1-1630 Chain F 1–1630（1630 aa） Fragment：residues 1-1630 Chain G 1–1630（1630 aa） Fragment：residues 1-1630 Chain H 1–1630（1630 aa） Fragment：residues 1-1630 Chain I 1–1630（1630 aa） Fragment：residues 1-1630	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 25mM MES；pH 6.5；25mM MES cryo-EM vitrification conditions Cryogen ETHANE；VITRIFIED	Resolution 7.90 Å
1XI4 Clathrin D6 Coat Deposited 2004-09-21	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric	Chain A 1–1630（1630 aa） Fragment：residues 1-1630 Chain B 1–1630（1630 aa） Fragment：residues 1-1630 Chain C 1–1630（1630 aa） Fragment：residues 1-1630 Chain D 1–1630（1630 aa） Fragment：residues 1-1630 Chain E 1–1630（1630 aa） Fragment：residues 1-1630 Chain F 1–1630（1630 aa） Fragment：residues 1-1630 Chain G 1–1630（1630 aa） Fragment：residues 1-1630 Chain H 1–1630（1630 aa） Fragment：residues 1-1630 Chain I 1–1630（1630 aa） Fragment：residues 1-1630	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 25mM MES；pH 6.5；25mM MES cryo-EM vitrification conditions Cryogen ETHANE；VITRIFIED	Resolution 7.90 Å
1XI4 Clathrin D6 Coat Deposited 2004-09-21	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric	Chain A 1–1630（1630 aa） Fragment：residues 1-1630 Chain B 1–1630（1630 aa） Fragment：residues 1-1630 Chain C 1–1630（1630 aa） Fragment：residues 1-1630 Chain D 1–1630（1630 aa） Fragment：residues 1-1630 Chain E 1–1630（1630 aa） Fragment：residues 1-1630 Chain F 1–1630（1630 aa） Fragment：residues 1-1630 Chain G 1–1630（1630 aa） Fragment：residues 1-1630 Chain H 1–1630（1630 aa） Fragment：residues 1-1630 Chain I 1–1630（1630 aa） Fragment：residues 1-1630	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 25mM MES；pH 6.5；25mM MES cryo-EM vitrification conditions Cryogen ETHANE；VITRIFIED	Resolution 7.90 Å
1XI5 Clathrin D6 coat with auxilin J-domain Deposited 2004-09-21	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 216 PDB declaration: 216-MERIC	Chain A 1–1630（1630 aa） Fragment：residues 1-1630 Chain B 1–1630（1630 aa） Fragment：residues 1-1630 Chain C 1–1630（1630 aa） Fragment：residues 1-1630 Chain D 1–1630（1630 aa） Fragment：residues 1-1630 Chain E 1–1630（1630 aa） Fragment：residues 1-1630 Chain F 1–1630（1630 aa） Fragment：residues 1-1630 Chain G 1–1630（1630 aa） Fragment：residues 1-1630 Chain H 1–1630（1630 aa） Fragment：residues 1-1630 Chain I 1–1630（1630 aa） Fragment：residues 1-1630	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20MM HEPES；pH 7；20MM HEPES cryo-EM vitrification conditions Cryogen ETHANE；VITRIFIED	Resolution 12.00 Å
1XI5 Clathrin D6 coat with auxilin J-domain Deposited 2004-09-21	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric	Chain A 1–1630（1630 aa） Fragment：residues 1-1630 Chain B 1–1630（1630 aa） Fragment：residues 1-1630 Chain C 1–1630（1630 aa） Fragment：residues 1-1630 Chain D 1–1630（1630 aa） Fragment：residues 1-1630 Chain E 1–1630（1630 aa） Fragment：residues 1-1630 Chain F 1–1630（1630 aa） Fragment：residues 1-1630 Chain G 1–1630（1630 aa） Fragment：residues 1-1630 Chain H 1–1630（1630 aa） Fragment：residues 1-1630 Chain I 1–1630（1630 aa） Fragment：residues 1-1630	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20MM HEPES；pH 7；20MM HEPES cryo-EM vitrification conditions Cryogen ETHANE；VITRIFIED	Resolution 12.00 Å
1XI5 Clathrin D6 coat with auxilin J-domain Deposited 2004-09-21	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric	Chain A 1–1630（1630 aa） Fragment：residues 1-1630 Chain B 1–1630（1630 aa） Fragment：residues 1-1630 Chain C 1–1630（1630 aa） Fragment：residues 1-1630 Chain D 1–1630（1630 aa） Fragment：residues 1-1630 Chain E 1–1630（1630 aa） Fragment：residues 1-1630 Chain F 1–1630（1630 aa） Fragment：residues 1-1630 Chain G 1–1630（1630 aa） Fragment：residues 1-1630 Chain H 1–1630（1630 aa） Fragment：residues 1-1630 Chain I 1–1630（1630 aa） Fragment：residues 1-1630	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20MM HEPES；pH 7；20MM HEPES cryo-EM vitrification conditions Cryogen ETHANE；VITRIFIED	Resolution 12.00 Å
3GC3 Crystal Structure of Arrestin2S and Clathrin Deposited 2009-02-21	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–363（363 aa） Fragment：WD domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；100 mM bis_tris propane 4 -4.5 M ammonium acetate 4.5% ethylene glycol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.20 Å R-free 0.251
3GD1 Structure of an Arrestin/Clathrin complex reveals a novel clathrin binding domain that modulates receptor trafficking Deposited 2009-02-23	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain I 1–363（363 aa） Fragment：WD domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 9；293 K；100mM Bicine, 7% O-(2-aminopropyl)-O'-(2-methoxyethyl)polypropylene glycol 500, 6% polyethylene glycol 8000, 4% acetone, 1% ethylene glycol and 10 mM strontium chloride, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.50 Å R-free 0.254
3IYV Clathrin D6 coat as full-length Triskelions Deposited 2010-06-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 216 PDB declaration: 216-meric	Chain A 1–1630（1630 aa） Fragment：UNP residues 1-1630 Chain B 1–1630（1630 aa） Fragment：UNP residues 1-1630 Chain C 1–1630（1630 aa） Fragment：UNP residues 1-1630 Chain D 1–1630（1630 aa） Fragment：UNP residues 1-1630 Chain E 1–1630（1630 aa） Fragment：UNP residues 1-1630 Chain F 1–1630（1630 aa） Fragment：UNP residues 1-1630 Chain G 1–1630（1630 aa） Fragment：UNP residues 1-1630 Chain H 1–1630（1630 aa） Fragment：UNP residues 1-1630 Chain I 1–1630（1630 aa） Fragment：UNP residues 1-1630	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 25MM MES；pH 6.5；25MM MES cryo-EM vitrification conditions Cryogen ETHANE；VITRIFIED	Resolution 7.90 Å
3IYV Clathrin D6 coat as full-length Triskelions Deposited 2010-06-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric	Chain A 1–1630（1630 aa） Fragment：UNP residues 1-1630 Chain B 1–1630（1630 aa） Fragment：UNP residues 1-1630 Chain C 1–1630（1630 aa） Fragment：UNP residues 1-1630 Chain D 1–1630（1630 aa） Fragment：UNP residues 1-1630 Chain E 1–1630（1630 aa） Fragment：UNP residues 1-1630 Chain F 1–1630（1630 aa） Fragment：UNP residues 1-1630 Chain G 1–1630（1630 aa） Fragment：UNP residues 1-1630 Chain H 1–1630（1630 aa） Fragment：UNP residues 1-1630 Chain I 1–1630（1630 aa） Fragment：UNP residues 1-1630	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 25MM MES；pH 6.5；25MM MES cryo-EM vitrification conditions Cryogen ETHANE；VITRIFIED	Resolution 7.90 Å
3IYV Clathrin D6 coat as full-length Triskelions Deposited 2010-06-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric	Chain A 1–1630（1630 aa） Fragment：UNP residues 1-1630 Chain B 1–1630（1630 aa） Fragment：UNP residues 1-1630 Chain C 1–1630（1630 aa） Fragment：UNP residues 1-1630 Chain D 1–1630（1630 aa） Fragment：UNP residues 1-1630 Chain E 1–1630（1630 aa） Fragment：UNP residues 1-1630 Chain F 1–1630（1630 aa） Fragment：UNP residues 1-1630 Chain G 1–1630（1630 aa） Fragment：UNP residues 1-1630 Chain H 1–1630（1630 aa） Fragment：UNP residues 1-1630 Chain I 1–1630（1630 aa） Fragment：UNP residues 1-1630	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 25MM MES；pH 6.5；25MM MES cryo-EM vitrification conditions Cryogen ETHANE；VITRIFIED	Resolution 7.90 Å
3LVG Crystal structure of a clathrin heavy chain and clathrin light chain complex Deposited 2010-02-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 1074–1675（602 aa） Chain B 1074–1675（602 aa） Chain C 1074–1675（602 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；200mM citrate, 16-22% glycerol, 2% trifluoroethanol, vapor diffusion, hanging drop, temperature 298K	Resolution 7.94 Å R-free 0.425
3LVH Crystal structure of a clathrin heavy chain and clathrin light chain complex Deposited 2010-02-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 1074–1675（602 aa） Fragment：Hub Chain B 1074–1675（602 aa） Fragment：Hub Chain C 1074–1675（602 aa） Fragment：Hub	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；200mM citrate, 16-22% glycerol, 2% trifluoroethanol, vapor diffusion, hanging drop, temperature 298K	Resolution 9.00 Å R-free 0.487
3QIL Crystal structure analysis of the clathrin trimerization domain Deposited 2011-01-27	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1521–1624（104 aa） Fragment：CLATHRIN TRIMERIZATION DOMAIN Chain B 1521–1624（104 aa） Fragment：CLATHRIN TRIMERIZATION DOMAIN Chain C 1521–1624（104 aa） Fragment：CLATHRIN TRIMERIZATION DOMAIN	Mutation：C1528A, T1585L Mutation：C1528A, T1585L Mutation：C1528A, T1585L	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；NaCl, Imidazole, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.92 Å R-free 0.386
3QIL Crystal structure analysis of the clathrin trimerization domain Deposited 2011-01-27	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain D 1521–1624（104 aa） Fragment：CLATHRIN TRIMERIZATION DOMAIN Chain E 1521–1624（104 aa） Fragment：CLATHRIN TRIMERIZATION DOMAIN Chain F 1521–1624（104 aa） Fragment：CLATHRIN TRIMERIZATION DOMAIN	Mutation：C1528A, T1585L Mutation：C1528A, T1585L Mutation：C1528A, T1585L	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；NaCl, Imidazole, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.92 Å R-free 0.386
3QIL Crystal structure analysis of the clathrin trimerization domain Deposited 2011-01-27	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain G 1521–1624（104 aa） Fragment：CLATHRIN TRIMERIZATION DOMAIN Chain H 1521–1624（104 aa） Fragment：CLATHRIN TRIMERIZATION DOMAIN Chain I 1521–1624（104 aa） Fragment：CLATHRIN TRIMERIZATION DOMAIN	Mutation：C1528A, T1585L Mutation：C1528A, T1585L Mutation：C1528A, T1585L	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；NaCl, Imidazole, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.92 Å R-free 0.386
3QIL Crystal structure analysis of the clathrin trimerization domain Deposited 2011-01-27	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain J 1521–1624（104 aa） Fragment：CLATHRIN TRIMERIZATION DOMAIN Chain K 1521–1624（104 aa） Fragment：CLATHRIN TRIMERIZATION DOMAIN Chain L 1521–1624（104 aa） Fragment：CLATHRIN TRIMERIZATION DOMAIN	Mutation：C1528A, T1585L Mutation：C1528A, T1585L Mutation：C1528A, T1585L	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；NaCl, Imidazole, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.92 Å R-free 0.386
3QIL Crystal structure analysis of the clathrin trimerization domain Deposited 2011-01-27	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain M 1521–1624（104 aa） Fragment：CLATHRIN TRIMERIZATION DOMAIN Chain N 1521–1624（104 aa） Fragment：CLATHRIN TRIMERIZATION DOMAIN Chain O 1521–1624（104 aa） Fragment：CLATHRIN TRIMERIZATION DOMAIN	Mutation：C1528A, T1585L Mutation：C1528A, T1585L Mutation：C1528A, T1585L	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；NaCl, Imidazole, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.92 Å R-free 0.386
3QIL Crystal structure analysis of the clathrin trimerization domain Deposited 2011-01-27	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 6 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain P 1521–1624（104 aa） Fragment：CLATHRIN TRIMERIZATION DOMAIN Chain Q 1521–1624（104 aa） Fragment：CLATHRIN TRIMERIZATION DOMAIN Chain R 1521–1624（104 aa） Fragment：CLATHRIN TRIMERIZATION DOMAIN	Mutation：C1528A, T1585L Mutation：C1528A, T1585L Mutation：C1528A, T1585L	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；NaCl, Imidazole, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.92 Å R-free 0.386
3QIL Crystal structure analysis of the clathrin trimerization domain Deposited 2011-01-27	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 7 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain S 1521–1624（104 aa） Fragment：CLATHRIN TRIMERIZATION DOMAIN Chain T 1521–1624（104 aa） Fragment：CLATHRIN TRIMERIZATION DOMAIN Chain U 1521–1624（104 aa） Fragment：CLATHRIN TRIMERIZATION DOMAIN	Mutation：C1528A, T1585L Mutation：C1528A, T1585L Mutation：C1528A, T1585L	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；NaCl, Imidazole, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.92 Å R-free 0.386
3QIL Crystal structure analysis of the clathrin trimerization domain Deposited 2011-01-27	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 8 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain V 1521–1624（104 aa） Fragment：CLATHRIN TRIMERIZATION DOMAIN Chain W 1521–1624（104 aa） Fragment：CLATHRIN TRIMERIZATION DOMAIN Chain X 1521–1624（104 aa） Fragment：CLATHRIN TRIMERIZATION DOMAIN	Mutation：C1528A, T1585L Mutation：C1528A, T1585L Mutation：C1528A, T1585L	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；NaCl, Imidazole, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.92 Å R-free 0.386
5M5R Clathrin heavy chain N-terminal domain bound to beta2 adaptin clathrin box motif Deposited 2016-10-22	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–363（363 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.7；293 K；1 uL protein plus peptide mix (14 mg/mL NTD and 3.4 mM peptide) plus 2 uL reservoir equilibrated against a 200 uL reservoir of 0.94 M sodium malonate pH 6.7	Resolution 1.76 Å R-free 0.205
5M5S Clathrin heavy chain N-terminal domain bound to amphiphysin clathrin-box motif Deposited 2016-10-22	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–363（363 aa）	Not recorded	GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；1 uL protein:peptide mix (14 mg/mL NTD and 3.4 mM peptide) plus 2 uL reservoir equilibrated against a 200 uL reservoir of 0.85 M sodium malonate pH 7.5	Resolution 1.88 Å R-free 0.234
5M5S Clathrin heavy chain N-terminal domain bound to amphiphysin clathrin-box motif Deposited 2016-10-22	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–363（363 aa）	Not recorded	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；1 uL protein:peptide mix (14 mg/mL NTD and 3.4 mM peptide) plus 2 uL reservoir equilibrated against a 200 uL reservoir of 0.85 M sodium malonate pH 7.5	Resolution 1.88 Å R-free 0.234
5M5T Clathrin heavy chain N-terminal domain bound to a non-natural clathrin-box motif peptide (Amph4T1) Deposited 2016-10-22	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 1–363（363 aa）	Not recorded	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；293 K；1 uL protein:peptide mix (14 mg/mL NTD and 3.4 mM peptide) plus 1 uL reservoir equilibrated against a 200 uL reservoir of 1.1 M sodium malonate pH 8.0	Resolution 1.70 Å R-free 0.185
5M5T Clathrin heavy chain N-terminal domain bound to a non-natural clathrin-box motif peptide (Amph4T1) Deposited 2016-10-22	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 1–363（363 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；293 K；1 uL protein:peptide mix (14 mg/mL NTD and 3.4 mM peptide) plus 1 uL reservoir equilibrated against a 200 uL reservoir of 1.1 M sodium malonate pH 8.0	Resolution 1.70 Å R-free 0.185
5M5U Clathrin heavy chain N-terminal domain bound to a clathrin-box motif from hepatitis D virus large antigen (clade 1) Deposited 2016-10-22	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–363（363 aa）	Not recorded	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；293 K；400 nL protein:peptide mix (14 mg/mL NTD and 3.4 mM) plus 200 nL reservoir equilibrated against a 80 uL reservoir of 1.21 M sodium malonate pH 7.0	Resolution 2.15 Å R-free 0.207
5M5U Clathrin heavy chain N-terminal domain bound to a clathrin-box motif from hepatitis D virus large antigen (clade 1) Deposited 2016-10-22	Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–363（363 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；293 K；400 nL protein:peptide mix (14 mg/mL NTD and 3.4 mM) plus 200 nL reservoir equilibrated against a 80 uL reservoir of 1.21 M sodium malonate pH 7.0	Resolution 2.15 Å R-free 0.207
5M5V Clathrin heavy chain N-terminal domain bound to a clathrin-box motif from hepatitis D virus large antigen (clade 2) Deposited 2016-10-22	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 1–363（363 aa）	Not recorded	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；293 K；200 nL protein:peptide (20 mg/mL NTD and 3.6 mM peptide) plus 400 nL reservoir equilibrated against a 80 uL reservoir of 1.75 M sodium malonate pH 7.0	Resolution 1.96 Å R-free 0.193
5M5V Clathrin heavy chain N-terminal domain bound to a clathrin-box motif from hepatitis D virus large antigen (clade 2) Deposited 2016-10-22	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 1–363（363 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；293 K；200 nL protein:peptide (20 mg/mL NTD and 3.6 mM peptide) plus 400 nL reservoir equilibrated against a 80 uL reservoir of 1.75 M sodium malonate pH 7.0	Resolution 1.96 Å R-free 0.193
5M61 Clathrin heavy chain N-terminal domain bound to an extended amphiphysin clathrin-box motif Deposited 2016-10-23	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–363（363 aa）	Not recorded	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.1；293 K；1 uL protein:peptide mix (14 mg/mL protein, 3.4 mM peptide) plus 2 uL of 1.04 M sodium malonate pH 7.1, 0.2 M sodium perchlorate equilibrated against a 200 uL reservoir of 1.15 M sodium malonate pH 7.1	Resolution 1.84 Å R-free 0.182
5M61 Clathrin heavy chain N-terminal domain bound to an extended amphiphysin clathrin-box motif Deposited 2016-10-23	Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–363（363 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.1；293 K；1 uL protein:peptide mix (14 mg/mL protein, 3.4 mM peptide) plus 2 uL of 1.04 M sodium malonate pH 7.1, 0.2 M sodium perchlorate equilibrated against a 200 uL reservoir of 1.15 M sodium malonate pH 7.1	Resolution 1.84 Å R-free 0.182
6WCJ Asymmetric vertex of the clathrin minicoat cage Deposited 2020-03-30	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: pentadecameric	Chain A 1–1675（1675 aa） Chain C 1–1675（1675 aa） Chain D 1–1675（1675 aa） Chain G 1–1675（1675 aa） Chain H 1–1675（1675 aa） Chain I 1–1675（1675 aa） Chain K 1–1675（1675 aa） Chain L 1–1675（1675 aa） Chain M 1–1675（1675 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.30 Å

17 other PDB entries and 36 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CLH1_BOVIN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–363； UniProt 1–363

AP2-associated protein kinase 1

OrganismNot specified

UniProt Q2M2I8

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain D； UniProt 956–961 Chain E； UniProt 956–961	Not recorded	Clathrin heavy chain 1 × 1 （P49951）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6；293.15 K；20% PEG 3,350; 100 mM Bis-Tris propane, pH 6.0; 200 mM sodium citrate; 10 mM DTT	Resolution 1.71 Å R-free 0.209

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 9F8T	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
4WSQ Crystal Structure of Adaptor Protein 2 Associated Kinase (AAK1) in complex with small molecule inhibitor Deposited 2014-10-28	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 29–345（317 aa） Fragment：kinase domain, UNP residues 29-345	Not recorded	ZN ZINC ION × 3 EDO 1,2-ETHANEDIOL × 1 KSA K-252A × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；0.005M zinc acetate, 20% PEG3350	Resolution 1.95 Å R-free 0.208
4WSQ Crystal Structure of Adaptor Protein 2 Associated Kinase (AAK1) in complex with small molecule inhibitor Deposited 2014-10-28	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 29–345（317 aa） Fragment：kinase domain, UNP residues 29-345	Not recorded	ZN ZINC ION × 3 KSA K-252A × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；0.005M zinc acetate, 20% PEG3350	Resolution 1.95 Å R-free 0.208
5L4Q Crystal Structure of Adaptor Protein 2 Associated Kinase 1 (AAK1) in Complex with LKB1 (AAK1 Dual Inhibitor) Deposited 2016-05-26	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 27–365（339 aa）	Not recorded	LKB ~{N}-[5-(4-cyanophenyl)-1~{H}-pyrrolo[2,3-b]pyridin-3-yl]pyridine-3-carboxamide × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；0.1M bis-tris pH 5.5, 26% PEG3350	Resolution 1.97 Å R-free 0.227
5L4Q Crystal Structure of Adaptor Protein 2 Associated Kinase 1 (AAK1) in Complex with LKB1 (AAK1 Dual Inhibitor) Deposited 2016-05-26	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 27–365（339 aa）	Not recorded	LKB ~{N}-[5-(4-cyanophenyl)-1~{H}-pyrrolo[2,3-b]pyridin-3-yl]pyridine-3-carboxamide × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；0.1M bis-tris pH 5.5, 26% PEG3350	Resolution 1.97 Å R-free 0.227
5TE0 Crystal Structure of Adaptor Protein 2 Associated Kinase (AAK1) in complex with BIBF 1120 Deposited 2016-09-20	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 27–365（339 aa） Fragment：UNP residues 27-365	Not recorded	XIN methyl (3Z)-3-{[(4-{methyl[(4-methylpiperazin-1-yl)acetyl]amino}phenyl)amino](phenyl)methylidene}-2-oxo-2,3-dihydro-1H-indole-6-carboxylate × 1 PEG DI(HYDROXYETHYL)ETHER × 1 GOL GLYCEROL × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；25 % PEG 3350, 0.1M BIS-TRIS, 0.2M Lithium Sulfate	Resolution 1.90 Å R-free 0.199
8GMC CRYSTAL STRUCTURE OF AP2 ASSOCIATED KINASE 1 COMPLEXED WITH 5-[(4-aminopiperidin-1-yl)methyl]-N-{3-[5-(propan-2-yl)-1,3,4-thiadiazol-2-yl]phenyl}pyrrolo[2,1-f][1,2,4]triazin-4-amine Deposited 2023-03-24	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 26–330（305 aa）	Not recorded	YFV 5-[(4-aminopiperidin-1-yl)methyl]-N-{3-[5-(propan-2-yl)-1,3,4-thiadiazol-2-yl]phenyl}pyrrolo[2,1-f][1,2,4]triazin-4-amine × 1 SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；296 K；1.2M AmSO4, 0.1M tri-Na Citrate pH 6.0, 3% isopropanol, 296K	Resolution 2.50 Å R-free 0.256
8GMC CRYSTAL STRUCTURE OF AP2 ASSOCIATED KINASE 1 COMPLEXED WITH 5-[(4-aminopiperidin-1-yl)methyl]-N-{3-[5-(propan-2-yl)-1,3,4-thiadiazol-2-yl]phenyl}pyrrolo[2,1-f][1,2,4]triazin-4-amine Deposited 2023-03-24	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 26–330（305 aa）	Not recorded	YFV 5-[(4-aminopiperidin-1-yl)methyl]-N-{3-[5-(propan-2-yl)-1,3,4-thiadiazol-2-yl]phenyl}pyrrolo[2,1-f][1,2,4]triazin-4-amine × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；296 K；1.2M AmSO4, 0.1M tri-Na Citrate pH 6.0, 3% isopropanol, 296K	Resolution 2.50 Å R-free 0.256
8GMD CRYSTAL STRUCTURE OF AP2 ASSOCIATED KINASE 1 COMPLEXED WITH (5P)-3-({(8R)-5-[(4-aminopiperidin-1-yl)methyl]pyrrolo[2,1-f][1,2,4]triazin-4-yl}amino)-5-[2-(propan-2-yl)-2H-tetrazol-5-yl]phenol Deposited 2023-03-24	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 26–330（305 aa）	Not recorded	ZRR (5P)-3-({(8R)-5-[(4-aminopiperidin-1-yl)methyl]pyrrolo[2,1-f][1,2,4]triazin-4-yl}amino)-5-[2-(propan-2-yl)-2H-tetrazol-5-yl]phenol × 1 SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；296 K；1.2M AmSO4, 0.1M tri-Na Citrate pH 6.0, 3% isopropanol, 296K	Resolution 2.20 Å R-free 0.250
8GMD CRYSTAL STRUCTURE OF AP2 ASSOCIATED KINASE 1 COMPLEXED WITH (5P)-3-({(8R)-5-[(4-aminopiperidin-1-yl)methyl]pyrrolo[2,1-f][1,2,4]triazin-4-yl}amino)-5-[2-(propan-2-yl)-2H-tetrazol-5-yl]phenol Deposited 2023-03-24	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 26–330（305 aa）	Not recorded	ZRR (5P)-3-({(8R)-5-[(4-aminopiperidin-1-yl)methyl]pyrrolo[2,1-f][1,2,4]triazin-4-yl}amino)-5-[2-(propan-2-yl)-2H-tetrazol-5-yl]phenol × 1 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；296 K；1.2M AmSO4, 0.1M tri-Na Citrate pH 6.0, 3% isopropanol, 296K	Resolution 2.20 Å R-free 0.250
9F6S PDZ domain in complex with the peptide from AP2-associated protein kinase 1 Deposited 2024-05-02	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 B 956–961（6 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.2 M Sodium chloride, 2.0 M Ammonium sulfate, 0.1 M Sodium cacodylate 6.5	Resolution 1.00 Å R-free 0.213
9QB5 AP2-associated protein kinase 1 (AAK1) bound to CKJB68 Deposited 2025-02-28	Different construct 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 29–345（317 aa） Chain B 29–345（317 aa）	Not recorded	F7I ~{N}-(phenylmethyl)-7,10-dioxa-13,17,18,21-tetrazatetracyclo[12.5.2.1^{2,6}.0^{17,20}]docosa-1(20),2(22),3,5,14(21),15,18-heptaene-5-carboxamide × 2 SO4 SULFATE ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.4；293 K；0.2 M ammonium sulfate 30% PEG4000	Resolution 2.00 Å R-free 0.227

7 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	AAK1_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain D； PDBConstruct 1–6； UniProt 956–961 Author chain E； PDBConstruct 1–6； UniProt 956–961

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.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	9f8t
Deposition date deposition_date	2024-05-07
最后修订 last_revision	2025-05-21
Structure title title	Clathrin terminal domain complexed with C-terminus of AAK1L
Keywords keywords	membrane traffic, kinase, ENDOCYTOSIS; ENDOCYTOSIS
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	22.32 Å
Radius of gyration Rg (electron density) rg_electron	21.06 Å
Forward intensity I(0) i0	29183700.00
Molecular weight molecular_weight	41778.0 kDa
Excluded volume excluded_volume	52489 Å³
Envelope volume envelope_volume	61593 Å³
Hydration-shell volume shell_volume	24072 Å³
Envelope diameter envelope_diameter	73.0 Å
Shell Rg shell_rg	28.10 Å
Envelope Rg envelope_rg	21.28 Å
Shape Rg shape_rg	21.04 Å
Total Rg total_rg	22.01 Å
Total atoms total_atoms	2933
Residues n_residues	375
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	70.3 Å
Rg (real space) rg_real	22.21 Å
Rg uncertainty (real space) rg_real_error	0.36 Å
I(0) (real space) i0_real	2.9180e+07
I(0) uncertainty (real space) i0_real_error	3.4890e+05
Rg (reciprocal space) rg_reciprocal	22.24 Å
I(0) (reciprocal space) i0_reciprocal	29180000.0000
Solution quality estimate total_estimate	0.8916
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	28.8 Å
Skewness Skewness skewness	0.179
Kurtosis Kurtosis kurtosis	-0.408
Angular range angular_range	— – 0.3550 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	9382000.0000
Real-space data points n_real_points	67
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.904; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.884

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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	Clathrin heavy chain 1
Molecular weight formula_weight	40396.3 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	3368

MAQILPIRFQEHLQLQNLGINPANIGFSTLTMESDKFICIREKVGEQAQVVIIDMNDPSNPIRRPISADSAIMNPASKVIALKAGKTLQIFNIEMKSKMKAHTMTDDVTFWKWISLNTVALVTDNAVYHWSMEGESQPVKMFDRHSSLAGCQIINYRTDAKQKWLLLTGISAQQNRVVGAMQLYSVDRKVSQPIEGHAASFAQFKMEGNAEESTLFCFAVRGQAGGKLHIIEVGTPPTGNQPFPKKAVDVFFPPEAQNDFPVAMQISEKHDVVFLITKYGYIHLYDLETGTCIYMNRISGETIFVTAPHEATAGIIGVNRKGQVLSVCVEEENIIPYITNVLQNPDLALRMAVRNNLAGAEEL

来源 Source

来源生物 organism	Bos taurus
通用名 common_name	domestic cattle
NCBI Class编号 ncbi_taxonomy_id	9913
宿主生物 host_organism	Escherichia coli DH5[alpha]

Entity 2 Entity 2 polymer

Description description	AP2-associated protein kinase 1
Molecular weight formula_weight	715.8 kDa
EC 编号 ec_number	2.7.11.1
Source method src_method	syn
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,E

DQLIDL

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	384

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8. Citations (1)

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Unit-cell length a length_a	107.539 Å
Unit-cell length b length_b	130.860 Å
Unit-cell length c length_c	77.050 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	16

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

Resolution resolution	1.711 Å
Low-resolution limit resolution_low	28.264 Å
R factor r_factor	—
R_work r_work	0.1723
R_free r_free	0.2092

fit	/app/data/saxs_computation/f8/9f8t/9f8t.fit
pddf	/app/data/pr_computation/f8/9f8t/9f8t.pr.out
profile	/app/data/saxs_computation/f8/9f8t/9f8t.dat

Clathrin terminal domain complexed with C-terminus of AAK1L

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

Clathrin heavy chain 1

State in the Current Structure

Other States of the Same Protein in the Database

AP2-associated protein kinase 1

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)