1jq1

POTASSIUM CHANNEL (KCSA) OPEN GATE MODEL

Method: SOLUTION NMR Dmax: 57.4 Å Quality: GOOD

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

VOLTAGE-GATED POTASSIUM CHANNEL

Streptomyces lividans

UniProt P0A334

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 86–119 Chain B; UniProt 86–119 Chain C; UniProt 86–119 Chain D; UniProt 86–119 Fragment:INNER TRANSMEMBRANE SEGMENT (residues 86-119) No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;150 K;Ionic strength (raw mmCIF value) 20 mM CITRATE PHOSPHATE;Pressure 1 NMR measurement conditions:pH 4;150 K;Ionic strength (raw mmCIF value) 20 mM CITRATE PHOSPHATE;Pressure 1 NMR sample composition:1.0 MG/ML MIXED WITH METHANETHIOSULFONATE SPIN LABEL | THE SAMPLES WERE RECONSTITUTED INTO ASOLECTIN LIPOSOMES AT A 1:400 PROTEIN:LIPID RATIO Resolution not provided

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.

86 other PDB entries and 96 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KCSA_STRLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–34; UniProt 86–119 Author chain B; PDBConstruct 1–34; UniProt 86–119 Author chain C; PDBConstruct 1–34; UniProt 86–119 Author chain D; PDBConstruct 1–34; UniProt 86–119

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

SAXS profile for 1jq1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1jq1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1jq1
Deposition date deposition_date2001-08-03
Structure title titlePOTASSIUM CHANNEL (KCSA) OPEN GATE MODEL
Keywords keywordsPOTASSIUM CHANNEL, INTEGRAL MEMBRANE PROTEIN, OPEN STATE, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier18.05
Radius of gyration Rg (electron density) rg_electron17.57
Forward intensity I(0) i03148540.00
Molecular weight molecular_weight14437.0 kDa
Excluded volume excluded_volume18210 ų
Envelope volume envelope_volume11471 ų
Hydration-shell volume shell_volume7171 ų
Envelope diameter envelope_diameter56.3
Shell Rg shell_rg18.95
Envelope Rg envelope_rg16.48
Shape Rg shape_rg16.90
Total Rg total_rg17.77
Total atoms total_atoms
Residues n_residues
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax57.4
Rg (real space) rg_real18.01
Rg uncertainty (real space) rg_real_error0.25
I(0) (real space) i0_real3.1490e+06
I(0) uncertainty (real space) i0_real_error3.7680e+04
Rg (reciprocal space) rg_reciprocal18.02
I(0) (reciprocal space) i0_reciprocal3149000.0000
Solution quality estimate total_estimate0.8972
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary21.7
Skewness Skewness skewness0.209
Kurtosis Kurtosis kurtosis-0.328
Angular range angular_range— – 0.4400 −1
Current regularization parameter α current_alpha0.0037
Highest regularization parameter α highest_alpha182700.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.915; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.914

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1jq1a_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.14 — Gated ion channels
Superfamily Superfamily superfamilyf.14.1 — Voltage-gated ion channels
Family Family familyf.14.1.1 — Voltage-gated potassium channels
Domain ID domain_idd1jq1b_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.14 — Gated ion channels
Superfamily Superfamily superfamilyf.14.1 — Voltage-gated ion channels
Family Family familyf.14.1.1 — Voltage-gated potassium channels
Domain ID domain_idd1jq1c_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.14 — Gated ion channels
Superfamily Superfamily superfamilyf.14.1 — Voltage-gated ion channels
Family Family familyf.14.1.1 — Voltage-gated potassium channels
Domain ID domain_idd1jq1d_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.14 — Gated ion channels
Superfamily Superfamily superfamilyf.14.1 — Voltage-gated ion channels
Family Family familyf.14.1.1 — Voltage-gated potassium channels

8. Citations (4)

9. Files and Curves (10)