5y0b

PIG GASTRIC H+,K+ - ATPASE IN COMPLEX with BYK99

Method: ELECTRON CRYSTALLOGRAPHY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Potassium-transporting ATPase alpha chain 1

OrganismNot specified

UniProt P19156

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 2 Potassium-transporting ATPase subunit beta × 1 (P18434) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name ATP4A_PIG
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1034; UniProt 1–1034

Potassium-transporting ATPase subunit beta

OrganismNot specified

UniProt P18434

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 2 Potassium-transporting ATPase alpha chain 1 × 1 (P19156) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name ATP4B_PIG
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–290; UniProt 1–290

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id5y0b
Deposition date deposition_date2017-07-16
Structure title titlePIG GASTRIC H+,K+ - ATPASE IN COMPLEX with BYK99
Keywords keywords;ion pump, h+, k+-atpase, p-type atpase, membrane protein, Hydrolase, e2, aluminium fluoride, ATP-binding, hydrogen ion transport, ion transport, magnesium, membrane, metal-binding, nucleotide-binding, phosphoprotein, potassium, potassium transport, transmembrane, transport, disulfide bond, glycoprotein, signal-anchor ;; HYDROLASE
Experimental Method methodELECTRON CRYSTALLOGRAPHY
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

5y0b__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

5y0b__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

5y0b__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)44.88 Å
Rg (electron density)45.60 Å
Total Rg45.30 Å
Atom count9101
Residues1161
Excluded volume163430 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 5y0b__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (2)

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7. Citations (1)