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5u6y

Pseudo-atomic model of the CaMKIIa holoenzyme.

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

Calcium/calmodulin-dependent protein kinase type II subunit alpha

Rattus norvegicus

UniProt P11275

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 12 No other associated polymer Consistent with protein count

Other States of the Same Protein in the Database

Monomer

None

Homodimer

None

Homotetramer

None

Other homooligomers
5u6y

1 assemblies

Heteromeric or nucleic-acid complex
1cdm 1cm1 1cm1 1cm4 8syg 8t15

6 assemblies

View Construct and Data Evidence
UniProt name KCC2A_RAT
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 2–461； UniProt 13–472 Author chain B； PDBConstruct 2–461； UniProt 13–472 Author chain C； PDBConstruct 2–461； UniProt 13–472 Author chain D； PDBConstruct 2–461； UniProt 13–472 Author chain E； PDBConstruct 2–461； UniProt 13–472 Author chain F； PDBConstruct 2–461； UniProt 13–472 Author chain G； PDBConstruct 2–461； UniProt 13–472 Author chain H； PDBConstruct 2–461； UniProt 13–472 Author chain I； PDBConstruct 2–461； UniProt 13–472 Author chain J； PDBConstruct 2–461； UniProt 13–472 Author chain K； PDBConstruct 2–461； UniProt 13–472 Author chain L； PDBConstruct 2–461； UniProt 13–472

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_id5u6y
Deposition date deposition_date2016-12-09
Structure title titlePseudo-atomic model of the CaMKIIa holoenzyme.
Keywords keywords;Calcium/calmodulin-dependent kinase II (CaMKII), cell signaling, calcium, calmodulin (CaM), long-term potentiation (LTP), long-term depression (LTD), synaptic plasticity, cooperativity, electron microscopy (EM), single particle reconstruction, intrinsic disorder, TRANSFERASE ;; TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY
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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.

5u6y__assembly_1__model_1

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

Download this curve (.dat)

5u6y__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 109 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

5u6y__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）95.15 Å
Rg (electron density)96.23 Å
Total Rg95.90 Å
Atom count86921
Residues5508
Excluded volume777590 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 5u6y__assembly_1__model_1 dodecameric （12） 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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7. Citations (1)