1h5p

Solution structure of the human Sp100b SAND domain by heteronuclear NMR.

Method: SOLUTION NMR
▼

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

NUCLEAR AUTOANTIGEN SP100-B

HOMO SAPIENS

UniProt P23497

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 SP10_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–95; UniProt 595–688

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id1h5p
Deposition date deposition_date2001-05-24
Structure title titleSolution structure of the human Sp100b SAND domain by heteronuclear NMR.
Keywords keywordsTRANSCRIPTION, DNA BINDING, SP100B, SAND DOMAIN, KDWK, ANTIGEN, NUCLEAR PROTEIN, ALTERNATIVE SPLICING; NUCLEAR PROTEIN
Experimental Method methodSOLUTION NMR
▼

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.

1h5p__assembly_1__model_2

Assembly 1 · Model 2 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1h5p__assembly_1__model_2 | I(q)

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

1h5p__assembly_1__model_2 | 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)14.49 Å
Rg (electron density)13.17 Å
Total Rg14.65 Å
Atom count1569
Residues95
Excluded volume13911 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1h5p__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 2 1h5p__assembly_1__model_2 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 3 1h5p__assembly_1__model_3 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 4 1h5p__assembly_1__model_4 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 5 1h5p__assembly_1__model_5 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 6 1h5p__assembly_1__model_6 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 7 1h5p__assembly_1__model_7 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 8 1h5p__assembly_1__model_8 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 9 1h5p__assembly_1__model_9 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 10 1h5p__assembly_1__model_10 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (1)

▼

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1h5pa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.217 — SAND domain-like
Superfamily Superfamily superfamilyd.217.1 — SAND domain-like
Family Family familyd.217.1.1 — SAND domain

CATH v4.4 (1 domains)

Domain ID domain_id1h5pA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology390 — SAND domain
Homologous superfamily homologous superfamily10 — SAND domain-like
▶

7. Citations (3)