SAXSdb — 6uwm

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

Voltage-gated potassium channel

Aeropyrum pernix

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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 25–295 Chain B； UniProt 25–295 Chain C； UniProt 25–295 Chain D； UniProt 25–295	Fragment：UNP residues 25-295	No other associated polymer	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE；Blot for 4 seconds before plunging.	Resolution 5.90 Å

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 6UWM	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1ORQ X-ray structure of a voltage-dependent potassium channel in complex with an Fab Deposited 2003-03-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain C 31–253（223 aa） Fragment：KvAP	Mutation：Y46C	CD CADMIUM ION × 28 K POTASSIUM ION × 24	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；293 K；PEG400, Cadmium chloride, Sodium acetate, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 3.20 Å R-free 0.298
1ORQ X-ray structure of a voltage-dependent potassium channel in complex with an Fab Deposited 2003-03-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 24 PDB declaration: 24-meric	Chain C 31–253（223 aa） Fragment：KvAP	Mutation：Y46C	CD CADMIUM ION × 56 K POTASSIUM ION × 48	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；293 K；PEG400, Cadmium chloride, Sodium acetate, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 3.20 Å R-free 0.298
1ORS X-ray structure of the KvAP potassium channel voltage sensor in complex with an Fab Deposited 2003-03-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 33–160（128 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；PEG4000, Hepes, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.90 Å R-free 0.251
2A0L Crystal structure of KvAP-33H1 Fv complex Deposited 2005-06-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 20–259（240 aa） Fragment：KvAP K+ channel Chain B 20–259（240 aa） Fragment：KvAP K+ channel	Not recorded	K POTASSIUM ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；sodium citrate, Tric-HCl, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 3.90 Å R-free 0.392
2KYH Solution structure of the voltage-sensing domain of KvAP Deposited 2010-05-26	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–160（143 aa） Fragment：UNP Residues 18-160	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；318 K；Ionic strength (raw mmCIF value) 40；Pressure AMBIENT NMR sample composition 0.1-0.5 MM [U-98% 15N] ENTITY, 20 MM HEPES, 20 MM POTASSIUM CHLORIDE, 5 MM DIHEPTANOYL PHOSPHATIDYLCHOLINE, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.1-0.5 MM [U-100% 13C U- 100% 15N U-80% 2H] ENTITY, 20 MM HEPES, 20 MM POTASSIUM CHLORIDE, 5 MM DIHEPTANOYL PHOSPHATIDYLCHOLINE, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.1-0.5 MM [U-98% 13C U-98% 15N] ENTITY, 20 MM HEPES, 20 MM POTASSIUM CHLORIDE, 5 MM DIHEPTANOYL PHOSPHATIDYLCHOLINE, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.1-0.5 MM [13CH3/12CD2]-LEU,VAL,[13CH3]-ILE ENTITY, 20 MM HEPES, 20 MM POTASSIUM CHLORIDE, 5 MM DIHEPTANOYL PHOSPHATIDYLCHOLINE, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided

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

View Construct and Data Evidence

UniProt name	KVAP_AERPE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–273； UniProt 25–295 Author chain B； PDBConstruct 3–273； UniProt 25–295 Author chain C； PDBConstruct 3–273； UniProt 25–295 Author chain D； PDBConstruct 3–273； UniProt 25–295

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	6uwm
Deposition date deposition_date	2019-11-05
Structure title title	Single particle cryo-EM structure of KvAP
Keywords keywords	voltage-gated potassium channel, non-domain-swapped, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	34.45 Å
Radius of gyration Rg (electron density) rg_electron	34.01 Å
Forward intensity I(0) i0	110763000.00
Molecular weight molecular_weight	96504.0 kDa
Excluded volume excluded_volume	126360 Å³
Envelope volume envelope_volume	174720 Å³
Hydration-shell volume shell_volume	43521 Å³
Envelope diameter envelope_diameter	116.4 Å
Shell Rg shell_rg	39.70 Å
Envelope Rg envelope_rg	34.26 Å
Shape Rg shape_rg	34.02 Å
Total Rg total_rg	34.53 Å
Total atoms total_atoms	6828
Residues n_residues	884
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	111.1 Å
Rg (real space) rg_real	34.37 Å
Rg uncertainty (real space) rg_real_error	0.81 Å
I(0) (real space) i0_real	1.1080e+08
I(0) uncertainty (real space) i0_real_error	1.7160e+06
Rg (reciprocal space) rg_reciprocal	34.42 Å
I(0) (reciprocal space) i0_reciprocal	110800000.0000
Solution quality estimate total_estimate	0.8852
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	45.9 Å
Skewness Skewness skewness	0.255
Kurtosis Kurtosis kurtosis	-0.242
Angular range angular_range	— – 0.2300 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	11200000.0000
Real-space data points n_real_points	47
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.876; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.879

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	—

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

Resolution resolution	5.90 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	67000

Description description	Voltage-gated potassium channel
Molecular weight formula_weight	31649.2 kDa
Source method src_method	man
Copy count entity_count	4

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C,B,D
Atom count atom_count	6828

Single particle cryo-EM structure of KvAP

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

Voltage-gated potassium channel

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Aeropyrum pernix
NCBI Class编号 ncbi_taxonomy_id	56636
宿主生物 host_organism	Escherichia coli BL21(DE3)

fit	/app/data/saxs_computation/uw/6uwm/6uwm.fit
pddf	/app/data/pr_computation/uw/6uwm/6uwm.pr.out
profile	/app/data/saxs_computation/uw/6uwm/6uwm.dat