1x9x

Solution Structure of Dimeric SAM Domain from MAPKKK Ste11

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

Serine/threonine-protein kinase STE11

Saccharomyces cerevisiae

UniProt P23561

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 2 No other associated polymer Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name STE11_YEAST
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–68; UniProt 37–104 Author chain B; PDBConstruct 1–68; UniProt 37–104

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_id1x9x
Deposition date deposition_date2004-08-24
Structure title titleSolution Structure of Dimeric SAM Domain from MAPKKK Ste11
Keywords keywordsSAM domain, MAP kinase, Ste11, TRANSFERASE; TRANSFERASE
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.

1x9x__assembly_1__model_6

Assembly 1 · Model 6 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1x9x__assembly_1__model_6 | I(q)

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

1x9x__assembly_1__model_6 | 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)16.35 Å
Rg (electron density)15.40 Å
Total Rg16.49 Å
Atom count2088
Residues124
Excluded volume18606 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1x9x__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 2 1x9x__assembly_1__model_2 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 3 1x9x__assembly_1__model_3 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 4 1x9x__assembly_1__model_4 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 5 1x9x__assembly_1__model_5 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 6 1x9x__assembly_1__model_6 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 7 1x9x__assembly_1__model_7 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 8 1x9x__assembly_1__model_8 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 (1)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1x9xa_
Class classa — All alpha proteins
Fold Fold folda.60 — SAM domain-like
Superfamily Superfamily superfamilya.60.1 — SAM/Pointed domain
Family Family familya.60.1.2 — SAM (sterile alpha motif) domain
Domain ID domain_idd1x9xb_
Class classa — All alpha proteins
Fold Fold folda.60 — SAM domain-like
Superfamily Superfamily superfamilya.60.1 — SAM/Pointed domain
Family Family familya.60.1.2 — SAM (sterile alpha motif) domain

CATH v4.4 (2 domains)

Domain ID domain_id1x9xA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily50 — Transcription Factor, Ets-1
Domain ID domain_id1x9xB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily50 — Transcription Factor, Ets-1
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7. Citations (1)