1owa

Solution Structural Studies on Human Erythrocyte Alpha Spectrin N Terminal Tetramerization Domain

Method: SOLUTION NMR
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Spectrin alpha chain, erythrocyte

Homo sapiens

UniProt P02549

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 No other associated polymer Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name SPTA1_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–156; UniProt 1–156

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_id1owa
Deposition date deposition_date2003-03-28
Structure title titleSolution Structural Studies on Human Erythrocyte Alpha Spectrin N Terminal Tetramerization Domain
Keywords keywordstriple helical bundle, CYTOKINE; CYTOKINE
Experimental Method methodSOLUTION NMR
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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.

1owa__assembly_1__model_1

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

Download this curve (.dat)

1owa__assembly_1__model_1 | I(q)

10-2 10-1 105 106 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1owa__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)30.09 Å
Rg (electron density)29.94 Å
Total Rg30.54 Å
Atom count2597
Residues156
Excluded volume22974 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1owa__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 2 1owa__assembly_1__model_2 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 3 1owa__assembly_1__model_3 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 4 1owa__assembly_1__model_4 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 5 1owa__assembly_1__model_5 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 6 1owa__assembly_1__model_6 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 7 1owa__assembly_1__model_7 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 8 1owa__assembly_1__model_8 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 9 1owa__assembly_1__model_9 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 10 1owa__assembly_1__model_10 monomeric (1) 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 (1)

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6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1owaa_
Class classa — All alpha proteins
Fold Fold folda.7 — Spectrin repeat-like
Superfamily Superfamily superfamilya.7.1 — Spectrin repeat
Family Family familya.7.1.1 — Spectrin repeat

CATH v4.4 (2 domains)

Domain ID domain_id1owaA01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily170 —
Domain ID domain_id1owaA02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily60 —
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7. Citations (1)