1svj

The solution structure of the nucleotide binding domain of KdpB

Method: SOLUTION NMR Dmax: 52.4 Å Quality: GOOD

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

Potassium-transporting ATPase B chain

Escherichia coli

UniProt P03960

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 316–451 Fragment:N-terminal domain No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6;300 K;Ionic strength (raw mmCIF value) 100mM NACL;Pressure AMBIENT NMR sample composition:1.4MM KDPBN U-15N,13C, 50MM PHOSPHATE BUFFER, 100MM NACL, 0.05% SODIUM AZIDE; 1.2MM KDPBN U-15N, 50MM PHOSPHATE BUFFER, 100MM NACL, 0.05% SODIUM AZIDE 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.

26 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATKB_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 21–156; UniProt 316–451

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 1svj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1svj
Deposition date deposition_date2004-03-29
Structure title titleThe solution structure of the nucleotide binding domain of KdpB
Keywords keywordsalpha-beta sandwich, HYDROLASE; HYDROLASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.45
Radius of gyration Rg (electron density) rg_electron13.92
Forward intensity I(0) i04680720.00
Molecular weight molecular_weight14800.0 kDa
Excluded volume excluded_volume18372 ų
Envelope volume envelope_volume20732 ų
Hydration-shell volume shell_volume12495 ų
Envelope diameter envelope_diameter50.4
Shell Rg shell_rg19.85
Envelope Rg envelope_rg14.55
Shape Rg shape_rg13.91
Total Rg total_rg15.15
Total atoms total_atoms2098
Residues n_residues136
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 dmax52.4
Rg (real space) rg_real15.36
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real4.6810e+06
I(0) uncertainty (real space) i0_real_error5.2130e+04
Rg (reciprocal space) rg_reciprocal15.37
I(0) (reciprocal space) i0_reciprocal4681000.0000
Solution quality estimate total_estimate0.8576
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.6
Skewness Skewness skewness0.200
Kurtosis Kurtosis kurtosis-0.182
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1343000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.727; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.966

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1svja_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.220 — Metal cation-transporting ATPase, ATP-binding domain N
Superfamily Superfamily superfamilyd.220.1 — Metal cation-transporting ATPase, ATP-binding domain N
Family Family familyd.220.1.1 — Metal cation-transporting ATPase, ATP-binding domain N

CATH v4.4 (1 domains)

Domain ID domain_id1svjA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1110 — Calcium-transporting ATPase, cytoplasmic domain N
Homologous superfamily homologous superfamily10 — Calcium-transporting ATPase, cytoplasmic domain N

8. Citations (1)

9. Files and Curves (10)