1k1g

STRUCTURAL BASIS FOR RECOGNITION OF THE INTRON BRANCH SITE RNA BY SPLICING FACTOR 1

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

SF1-Bo isoform

Homo sapiens

UniProt Q15637

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–RNA Monomer Protein 1 RNA 1 5'-R(*UP*AP*UP*AP*CP*UP*AP*AP*CP*AP*A)-3' × 1 Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name SF01_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 4–131; UniProt 133–260

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_id1k1g
Deposition date deposition_date2001-09-25
Structure title titleSTRUCTURAL BASIS FOR RECOGNITION OF THE INTRON BRANCH SITE RNA BY SPLICING FACTOR 1
Keywords keywords;Splicing, branch point sequence, protein/RNA recognition, complex E, KH domain, QUA2 homology, STAR proteins, GENE REGULATION-RNA COMPLEX ;; GENE REGULATION/RNA
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.

1k1g__assembly_1__model_1

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

Download this curve (.dat)

1k1g__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.

1k1g__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)16.62 Å
Rg (electron density)15.24 Å
Total Rg16.32 Å
Atom count2308
Residues133
Excluded volume20368 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1k1g__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 2 1k1g__assembly_1__model_2 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 3 1k1g__assembly_1__model_3 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 4 1k1g__assembly_1__model_4 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 5 1k1g__assembly_1__model_5 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 6 1k1g__assembly_1__model_6 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 7 1k1g__assembly_1__model_7 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 8 1k1g__assembly_1__model_8 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 9 1k1g__assembly_1__model_9 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 10 1k1g__assembly_1__model_10 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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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1k1ga_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.51 — Eukaryotic type KH-domain (KH-domain type I)
Superfamily Superfamily superfamilyd.51.1 — Eukaryotic type KH-domain (KH-domain type I)
Family Family familyd.51.1.1 — Eukaryotic type KH-domain (KH-domain type I)

CATH v4.4 (1 domains)

Domain ID domain_id1k1gA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1370 — Ribosomal Protein S8; Chain: A, domain 1
Homologous superfamily homologous superfamily10 — K Homology domain, type 1
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7. Citations (1)