4msw

Y78 ester mutant of KcsA in high K+

Method: X-RAY DIFFRACTION Dmax: 125.3 Å Quality: REASONABLE

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

Monoclonal 11D8 anti-human butyrylcholinesterase (BChE) light chain

Mus musculus

UniProt A0A0M4KEQ7

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 21–232 Not recorded ANTIBODY FAB FRAGMENT HEAVY CHAIN × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;PEG400, Magnesium acetate, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 2.06 Å R-free 0.229

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A0M4KEQ7_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–212; UniProt 21–232

pH-gated potassium channel KcsA

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
2 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 22–76 Chain C; UniProt 78–124 Fragment:UNP residues 22-124,UNP residues 22-124 Non-standard monomer:Yes (specific site not provided by mmCIF) DGA DIACYL GLYCEROL × 4 K POTASSIUM ION × 24 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;PEG400, Magnesium acetate, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 2.06 Å R-free 0.229

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 3
Chains and sequence ranges Author chain C; PDBConstruct 1–55; UniProt 22–76 Author chain C; PDBConstruct 56–102; UniProt 78–124

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 4msw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4msw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4msw
Deposition date deposition_date2013-09-18
Structure title titleY78 ester mutant of KcsA in high K+
Keywords keywordsMembrane protein, Channel, Ester, Unnatural amino acid, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.31
Radius of gyration Rg (electron density) rg_electron30.80
Forward intensity I(0) i0102323000.00
Molecular weight molecular_weight54122.0 kDa
Excluded volume excluded_volume52613 ų
Envelope volume envelope_volume94565 ų
Hydration-shell volume shell_volume28398 ų
Envelope diameter envelope_diameter130.8
Shell Rg shell_rg34.00
Envelope Rg envelope_rg32.09
Shape Rg shape_rg30.77
Total Rg total_rg31.07
Total atoms total_atoms4094
Residues n_residues532
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 dmax125.3
Rg (real space) rg_real30.99
Rg uncertainty (real space) rg_real_error1.55
I(0) (real space) i0_real1.0230e+08
I(0) uncertainty (real space) i0_real_error1.6700e+06
Rg (reciprocal space) rg_reciprocal30.69
I(0) (reciprocal space) i0_reciprocal102300000.0000
Solution quality estimate total_estimate0.6959
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.9
Skewness Skewness skewness0.954
Kurtosis Kurtosis kurtosis0.950
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7802000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.300; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.194; Smooth: 0.949

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 11 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd4mswa1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd4mswa2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)
Domain ID domain_idd4mswa3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4mswb1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd4mswb2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)
Domain ID domain_idd4mswc_
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

CATH v4.4 (5 domains)

Domain ID domain_id4mswA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4mswA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4mswB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4mswB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4mswC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily70

8. Citations (1)

9. Files and Curves (10)