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1ztn

INACTIVATION GATE OF POTASSIUM CHANNEL RAW3, NMR, 8 STRUCTURES

Method: SOLUTION NMR Dmax: 27.4 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Potassium voltage-gated channel subfamily C member 4

Homo sapiens

UniProt Q03721

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–30 Fragment：INACTIVATION GATE, N-terminal No other associated polymer SOLUTION NMR NMR measurement conditions：pH 3.5；283 K 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.

Other PDB Difference from Current Entry 1ZTN Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1B4G CONTROL OF K+ CHANNEL GATING BY PROTEIN PHOSPHORYLATION: STRUCTURAL SWITCHES OF THE INACTIVATION GATE, NMR, 22 STRUCTURES Deposited 1998-12-22 Different construct Different mutation/modification Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–30（30 aa） Fragment：INACTIVATION DOMAIN
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3.5；283 K
Resolution not provided
1B4I Control of K+ Channel Gating by protein phosphorylation: structural switches of the inactivation gate, NMR, 22 structures Deposited 1998-12-22 Different construct Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–30（30 aa） Fragment：INACTIVATION GATE
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3.4；283 K
Resolution not provided

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KCNC4_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–30； UniProt 1–30

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 1ztn

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ztn
Deposition date deposition_date1996-11-15
Structure title titleINACTIVATION GATE OF POTASSIUM CHANNEL RAW3, NMR, 8 STRUCTURES
Keywords keywordsPOTASSIUM CHANNEL, INACTIVATION GATE, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier7.71 Å
Radius of gyration Rg (electron density) rg_electron8.04 Å
Forward intensity I(0) i011829700.00
Molecular weight molecular_weight26231.0 kDa
Excluded volume excluded_volume32290 ų
Envelope volume envelope_volume5526 ų
Hydration-shell volume shell_volume5693 ų
Envelope diameter envelope_diameter28.4 Å
Shell Rg shell_rg13.71 Å
Envelope Rg envelope_rg9.17 Å
Shape Rg shape_rg8.00 Å
Total Rg total_rg8.53 Å
Total atoms total_atoms3696
Residues n_residues240
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax27.4 Å
Rg (real space) rg_real7.70 Å
Rg uncertainty (real space) rg_real_error0.31 Å
I(0) (real space) i0_real1.1830e+07
I(0) uncertainty (real space) i0_real_error1.1980e+05
Rg (reciprocal space) rg_reciprocal7.70 Å
I(0) (reciprocal space) i0_reciprocal11830000.0000
Solution quality estimate total_estimate0.7640
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary9.4 Å
Skewness Skewness skewness0.331
Kurtosis Kurtosis kurtosis-0.008
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16750.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.662; Stabil: 0.991; Sysdev: 1.000; Positv: 1.000; Valcen: 0.969; Smooth: 0.000
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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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7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1ztna_
Class classj — Peptides
Fold Fold foldj.12 — Inactivation gate of potassium and sodium channels
Superfamily Superfamily superfamilyj.12.1 — Inactivation gate of potassium and sodium channels
Family Family familyj.12.1.1 — Inactivation gate of potassium and sodium channels
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8. Citations (1)

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9. Files and Curves (10)