SAXSdb — 4eqf

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

PEX5-related protein

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 206–567	Fragment：UNP residues 206-567	Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 × 1 （O88703）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6；298 K；91mM MES, 91mM triSodium citrate, 3.63M NaCL, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.00 Å R-free 0.281

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	PEX5R_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–365； UniProt 206–567

Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2

OrganismNot specified

UniProt O88703

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 857–863	Fragment：UNP residues 857-863	PEX5-related protein × 1 （Q8C437）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6；298 K；91mM MES, 91mM triSodium citrate, 3.63M NaCL, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.00 Å R-free 0.281

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 4EQF	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1Q3E HCN2J 443-645 in the presence of cGMP Deposited 2003-07-29	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 443–645（203 aa） Fragment：Residues 443-645 (Reference sequence numbering)	Not recorded	PCG CYCLIC GUANOSINE MONOPHOSPHATE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；277 K；PEG 400, sodium citrate, sodium chloride, DTT, HEPES, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.239
1Q3E HCN2J 443-645 in the presence of cGMP Deposited 2003-07-29	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain B 443–645（203 aa） Fragment：Residues 443-645 (Reference sequence numbering)	Not recorded	PCG CYCLIC GUANOSINE MONOPHOSPHATE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；277 K；PEG 400, sodium citrate, sodium chloride, DTT, HEPES, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.239
1Q3E HCN2J 443-645 in the presence of cGMP Deposited 2003-07-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 443–645（203 aa） Fragment：Residues 443-645 (Reference sequence numbering) Chain B 443–645（203 aa） Fragment：Residues 443-645 (Reference sequence numbering)	Not recorded	PCG CYCLIC GUANOSINE MONOPHOSPHATE × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；277 K；PEG 400, sodium citrate, sodium chloride, DTT, HEPES, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.239
1Q43 HCN2I 443-640 in the presence of cAMP, selenomethionine derivative Deposited 2003-08-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 443–645（203 aa） Fragment：residues 443-645	Non-standard monomer：Yes (specific site not provided by mmCIF)	CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；277 K；PEG 400, sodium citrate, sodium chloride, DTT, HEPES, cAMP, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.00 Å R-free 0.242
1Q43 HCN2I 443-640 in the presence of cAMP, selenomethionine derivative Deposited 2003-08-01	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 443–645（203 aa） Fragment：residues 443-645	Non-standard monomer：Yes (specific site not provided by mmCIF)	CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；277 K；PEG 400, sodium citrate, sodium chloride, DTT, HEPES, cAMP, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.00 Å R-free 0.242
1Q43 HCN2I 443-640 in the presence of cAMP, selenomethionine derivative Deposited 2003-08-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 443–645（203 aa） Fragment：residues 443-645 Chain B 443–645（203 aa） Fragment：residues 443-645	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；277 K；PEG 400, sodium citrate, sodium chloride, DTT, HEPES, cAMP, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.00 Å R-free 0.242
1Q43 HCN2I 443-640 in the presence of cAMP, selenomethionine derivative Deposited 2003-08-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain B 443–645（203 aa） Fragment：residues 443-645	Non-standard monomer：Yes (specific site not provided by mmCIF)	CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；277 K；PEG 400, sodium citrate, sodium chloride, DTT, HEPES, cAMP, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.00 Å R-free 0.242
1Q5O HCN2J 443-645 in the presence of cAMP, selenomethionine derivative Deposited 2003-08-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 443–645（203 aa） Fragment：Residues 443-645	Non-standard monomer：Yes (specific site not provided by mmCIF)	CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；277 K；PEG 400, sodium citrate, sodium chloride, DTT, HEPES, cAMP, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.30 Å R-free 0.261
2Q0A Structure and rearrangements in the carboxy-terminal region of SpIH channels Deposited 2007-05-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 443–640（198 aa） Fragment：C-TERMINAL DOMAIN (residues 443-640)	Mutation：I636D	PCG CYCLIC GUANOSINE MONOPHOSPHATE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；277 K；10 % w/v PEG 8000, 0.5 M NaCl, 15 % Glycerol, 0.1 M MES, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.25 Å R-free 0.261
2Q0A Structure and rearrangements in the carboxy-terminal region of SpIH channels Deposited 2007-05-21	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 443–640（198 aa） Fragment：C-TERMINAL DOMAIN (residues 443-640)	Mutation：I636D	PCG CYCLIC GUANOSINE MONOPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；277 K；10 % w/v PEG 8000, 0.5 M NaCl, 15 % Glycerol, 0.1 M MES, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.25 Å R-free 0.261
2Q0A Structure and rearrangements in the carboxy-terminal region of SpIH channels Deposited 2007-05-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 443–640（198 aa） Fragment：C-TERMINAL DOMAIN (residues 443-640) Chain B 443–640（198 aa） Fragment：C-TERMINAL DOMAIN (residues 443-640)	Mutation：I636D Mutation：I636D	PCG CYCLIC GUANOSINE MONOPHOSPHATE × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；277 K；10 % w/v PEG 8000, 0.5 M NaCl, 15 % Glycerol, 0.1 M MES, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.25 Å R-free 0.261
2Q0A Structure and rearrangements in the carboxy-terminal region of SpIH channels Deposited 2007-05-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain B 443–640（198 aa） Fragment：C-TERMINAL DOMAIN (residues 443-640)	Mutation：I636D	PCG CYCLIC GUANOSINE MONOPHOSPHATE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；277 K；10 % w/v PEG 8000, 0.5 M NaCl, 15 % Glycerol, 0.1 M MES, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.25 Å R-free 0.261
3BPZ HCN2-I 443-460 E502K in the presence of cAMP Deposited 2007-12-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 443–640（198 aa） Fragment：ligand biding domain (residues 443-640) Chain B 443–640（198 aa） Fragment：ligand biding domain (residues 443-640) Chain C 443–640（198 aa） Fragment：ligand biding domain (residues 443-640) Chain D 443–640（198 aa） Fragment：ligand biding domain (residues 443-640)	Mutation：E502K Mutation：E502K Mutation：E502K Mutation：E502K	CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 4.6；279 K；PEG 400, SODIUM CITRATE, SODIUM CHLORIDE, DTT, HEPES, 5 mM CAMP, pH 4.6, VAPOR DIFFUSION, temperature 279K	Resolution 1.65 Å R-free 0.216
3ETQ X-ray structure of cysteine-free fragment of mHCN2 C-terminal region from amino acids 443-630 including C508N, C584S, and C601S mutations Deposited 2008-10-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 443–640（198 aa） Fragment：C-terminal fragment Chain B 443–640（198 aa） Fragment：C-terminal fragment	Mutation：C508N, C584S, C601S Mutation：C508N, C584S, C601S	CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；277 K；16% w/v PEG 6000, 500 mM NaCl, 10% glycerol, 100 mM citrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.216
3FFQ HCN2I 443-640 apo-state Deposited 2008-12-04	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 443–640（198 aa）	Not recorded	BR BROMIDE ION × 20	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；Two uL protein (5-7 mg/mL) mixed with one uL reservoir solution composed of 0.4 M NaCl, 0.1 NaBr, 0.1 M MES, pH 6.0, 20% glycerol (v/v), and 20% PEG 8000 (w/v). Crystals grew within eight weeks and harvested an additional eight weeks after initial growth, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.40 Å R-free 0.283
3FFQ HCN2I 443-640 apo-state Deposited 2008-12-04	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain B 443–640（198 aa）	Not recorded	BR BROMIDE ION × 16	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；Two uL protein (5-7 mg/mL) mixed with one uL reservoir solution composed of 0.4 M NaCl, 0.1 NaBr, 0.1 M MES, pH 6.0, 20% glycerol (v/v), and 20% PEG 8000 (w/v). Crystals grew within eight weeks and harvested an additional eight weeks after initial growth, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.40 Å R-free 0.283
5JON Crystal structure of the unliganded form of HCN2 CNBD Deposited 2016-05-02	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 494–640（147 aa）	Not recorded	NO3 NITRATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；34-36% dimethyl PEG 500, 240 mM potassium nitrate, 20 mM magnesium chloride, 100 mM BIS-TRIS, pH 6.0	Resolution 2.04 Å R-free 0.221
5JON Crystal structure of the unliganded form of HCN2 CNBD Deposited 2016-05-02	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain B 494–640（147 aa）	Not recorded	NO3 NITRATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；34-36% dimethyl PEG 500, 240 mM potassium nitrate, 20 mM magnesium chloride, 100 mM BIS-TRIS, pH 6.0	Resolution 2.04 Å R-free 0.221
5KHG HCN2 CNBD in complex with cytidine-3', 5'-cyclic monophosphate (cCMP) Deposited 2016-06-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 443–643（201 aa） Fragment：UNP residues 443-643	Non-standard monomer：Yes (specific site not provided by mmCIF)	CC7 4-amino-1-[(2S,4aR,6R,7R,7aS)-2,7-dihydroxy-2-oxidotetrahydro-4H-furo[3,2-d][1,3,2]dioxaphosphinin-6-yl]pyrimidin-2(1H)-one × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；277 K；200 mM NaCl, 0.1 mM sodium citrate pH 5.0, 16% PEG 400	Resolution 2.24 Å R-free 0.264
5KHH HCN2 CNBD in complex with inosine-3', 5'-cyclic monophosphate (cIMP) Deposited 2016-06-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 443–643（201 aa） Fragment：UNP residues 443-643	Non-standard monomer：Yes (specific site not provided by mmCIF)	6SW Inosine-3',5'-cyclic monophosphate × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；200 mM NaCl, 0.1 mM sodium citrate pH 5.5, 14.5% PEG 400	Resolution 1.77 Å R-free 0.263
5KHI HCN2 CNBD in complex with purine riboside-3', 5'-cyclic monophosphate (cPuMP) Deposited 2016-06-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 443–643（201 aa） Fragment：UNP residues 443-643	Non-standard monomer：Yes (specific site not provided by mmCIF)	6SX Purine riboside-3',5'-cyclic monophosphate × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；200 mM NaCl, 0.1 mM sodium citrate pH 5.5, 18% PEG 400	Resolution 2.10 Å R-free 0.249
5KHJ HCN2 CNBD in complex with uridine-3', 5'-cyclic monophosphate (cUMP) Deposited 2016-06-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 443–643（201 aa） Fragment：UNP residues 443-643 Chain B 443–643（201 aa） Fragment：UNP residues 443-643	Not recorded	6SY Uridine-3',5'-cyclic monophosphate × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；277 K；200 mM NaCl, 0.1 mM sodium citrate pH 4.6, 13% PEG 400	Resolution 2.01 Å R-free 0.252
5KHK HCN2 CNBD in complex with 2-aminopurine riboside-3', 5'-cyclic monophosphate (2-NH2-cPuMP) Deposited 2016-06-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 443–643（201 aa） Fragment：UNP residues 443-643	Non-standard monomer：Yes (specific site not provided by mmCIF)	6SZ 2-Aminopurine riboside-3',5'-cyclic monophosphate × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；277 K；200 mM NaCl, 0.1 mM sodium citrate pH 4.6, 12% PEG 400	Resolution 2.07 Å R-free 0.261
9R1T Structure of the human chimera HCN112 hyperpolarization-activated cyclic nucleotide-gated ion channel in complex with cAMP. Deposited 2025-04-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 444–647（204 aa） Chain B 444–647（204 aa） Chain C 444–647（204 aa） Chain D 444–647（204 aa）	Not recorded	CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.34 Å

14 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	HCN2_MOUSE
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–7； UniProt 857–863

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	4eqf
Deposition date deposition_date	2012-04-18
Structure title title	Trip8b-1a#206-567 interacting with the carboxy-terminal seven residues of HCN2
Keywords keywords	;Accessory protein, Tetratricopeptide repeat, TPR, Accessory Protein for HCN channels, HCN, PROTEIN BINDING-TRANSPORT PROTEIN complex ;; PROTEIN BINDING/TRANSPORT 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	20.41 Å
Radius of gyration Rg (electron density) rg_electron	19.58 Å
Forward intensity I(0) i0	17976100.00
Molecular weight molecular_weight	32018.0 kDa
Excluded volume excluded_volume	40038 Å³
Envelope volume envelope_volume	46536 Å³
Hydration-shell volume shell_volume	19947 Å³
Envelope diameter envelope_diameter	68.5 Å
Shell Rg shell_rg	25.70 Å
Envelope Rg envelope_rg	19.98 Å
Shape Rg shape_rg	19.58 Å
Total Rg total_rg	20.43 Å
Total atoms total_atoms	2260
Residues n_residues	287
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	67.2 Å
Rg (real space) rg_real	20.35 Å
Rg uncertainty (real space) rg_real_error	0.53 Å
I(0) (real space) i0_real	1.7980e+07
I(0) uncertainty (real space) i0_real_error	2.2980e+05
Rg (reciprocal space) rg_reciprocal	20.36 Å
I(0) (reciprocal space) i0_reciprocal	17980000.0000
Solution quality estimate total_estimate	0.8101
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	25.0 Å
Skewness Skewness skewness	0.270
Kurtosis Kurtosis kurtosis	-0.338
Angular range angular_range	— – 0.3900 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	5229000.0000
Real-space data points n_real_points	71
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.845; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	PEX5-related protein
Molecular weight formula_weight	40969.9 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	2260

GAMEFERAKAAVESDTEFWDKMQAEWEEMARRNWISENQEAQNQVTVSASEKGYYFHTENPFKDWPGAFEEGLKRLKEGDLPVTILFMEAAILQDPGDAEAWQFLGITQAENENEQAAIVALQRCLELQPNNLKALMALAVSYTNTSHQQDACEALKNWIKQNPKYKYLVKNKKGSPGLTRRMSKSPVDSSVLEGVKELYLEAAHQNGDMIDPDLQTGLGVLFHLSGEFNRAIDAFNAALTVRPEDYSLWNRLGATLANGDRSEEAVEAYTRALEIQPGFIRSRYNLGISCINLGAYREAVSNFLTALSLQRKSRNQQQVPHPAISGNIWAALRIALSLMDQPELFQAANLGDLDVLLRAFNLDP

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	Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2
Molecular weight formula_weight	776.9 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

SRLSSNL

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	4eqfA00
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily	10 — Tetratricopeptide repeat domain

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8. Citations (1)

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Unit-cell length a length_a	72.320 Å
Unit-cell length b length_b	72.320 Å
Unit-cell length c length_c	146.740 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	8

Space group space_group	P 41 21 2
Space-group number int_tables_number	92
Crystal system crystal_system	—

Resolution resolution	3.000 Å
Low-resolution limit resolution_low	29.808 Å
R factor r_factor	0.2293
R_work r_work	0.2268
R_free r_free	0.2807

fit	/app/data/saxs_computation/eq/4eqf/4eqf.fit
pddf	/app/data/pr_computation/eq/4eqf/4eqf.pr.out
profile	/app/data/saxs_computation/eq/4eqf/4eqf.dat

Trip8b-1a#206-567 interacting with the carboxy-terminal seven residues of HCN2

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

PEX5-related protein

State in the Current Structure

Other States of the Same Protein in the Database

Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2

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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)