1b4i

Control of K+ Channel Gating by protein phosphorylation: structural switches of the inactivation gate, NMR, 22 structures

Method: SOLUTION NMR D_max: 25.6 Å Quality: REASONABLE

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

POTASSIUM CHANNEL

Homo sapiens

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 Non-standard monomer：Yes (specific site not provided by mmCIF)	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 3.4；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 1B4I	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 experimental conditions	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
1ZTN INACTIVATION GATE OF POTASSIUM CHANNEL RAW3, NMR, 8 STRUCTURES Deposited 1996-11-15	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, N-terminal	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.5；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

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	1b4i
Deposition date deposition_date	1998-12-22
Structure title title	Control of K+ Channel Gating by protein phosphorylation: structural switches of the inactivation gate, NMR, 22 structures
Keywords keywords	POTASSIUM CHANNEL, INACTIVATION GATE, PHOSPHORYLATION, PROTON TRANSPORT; PROTON TRANSPORT
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	9.77 Å
Radius of gyration Rg (electron density) rg_electron	9.99 Å
Forward intensity I(0) i0	120090000.00
Molecular weight molecular_weight	79139.0 kDa
Excluded volume excluded_volume	94833 Å³
Envelope volume envelope_volume	21989 Å³
Hydration-shell volume shell_volume	12801 Å³
Envelope diameter envelope_diameter	52.2 Å
Shell Rg shell_rg	20.51 Å
Envelope Rg envelope_rg	15.22 Å
Shape Rg shape_rg	9.90 Å
Total Rg total_rg	10.77 Å
Total atoms total_atoms	10810
Residues n_residues	644
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	25.6 Å
Rg (real space) rg_real	9.20 Å
Rg uncertainty (real space) rg_real_error	0.04 Å
I(0) (real space) i0_real	1.1500e+08
I(0) uncertainty (real space) i0_real_error	8.1800e+05
Rg (reciprocal space) rg_reciprocal	9.89 Å
I(0) (reciprocal space) i0_reciprocal	120100000.0000
Solution quality estimate total_estimate	0.6864
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	11.0 Å
Skewness Skewness skewness	0.293
Kurtosis Kurtosis kurtosis	-0.447
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	3.9120
Highest regularization parameter α highest_alpha	28960.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.001; Oscil: 0.996; Stabil: 0.980; Sysdev: 0.000; Positv: 1.000; Valcen: 0.997; 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_id	d1b4ia_
Class class	j — Peptides
Fold Fold fold	j.12 — Inactivation gate of potassium and sodium channels
Superfamily Superfamily superfamily	j.12.1 — Inactivation gate of potassium and sodium channels
Family Family family	j.12.1.1 — Inactivation gate of potassium and sodium channels

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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	1

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

Description description	POTASSIUM CHANNEL
Molecular weight formula_weight	3440.8 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	10810

来源生物 organism	Homo sapiens
NCBI Class编号 ncbi_taxonomy_id	9606

Control of K+ Channel Gating by protein phosphorylation: structural switches of the inactivation gate, NMR, 22 structures

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

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

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/b4/1b4i/1b4i.fit
pddf	/app/data/pr_computation/b4/1b4i/1b4i.pr.out
profile	/app/data/saxs_computation/b4/1b4i/1b4i.dat