5m5c

Mechanism of microtubule minus-end recognition and protection by CAMSAP proteins

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

Calmodulin-regulated spectrin-associated protein 1

Homo sapiens

UniProt Q5T5Y3

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 5 Tubulin alpha chain × 2 (F2Z4C1) Tubulin beta-2B chain × 2 (Q6B856) GUANOSINE-5'-TRIPHOSPHATE × 2 MAGNESIUM ION × 2 GUANOSINE-5'-DIPHOSPHATE × 2 TAXOL × 2 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name CAMP1_HUMAN
Isoform Q5T5Y3-3
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 1–118; UniProt 1483–1600

Tubulin alpha chain

OrganismNot specified

UniProt F2Z4C1

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 5 Calmodulin-regulated spectrin-associated protein 1 × 1 (Q5T5Y3) Tubulin beta-2B chain × 2 (Q6B856) GUANOSINE-5'-TRIPHOSPHATE × 2 MAGNESIUM ION × 2 GUANOSINE-5'-DIPHOSPHATE × 2 TAXOL × 2 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name F2Z4C1_BOVIN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–438; UniProt 2–439 Author chain D; PDBConstruct 1–438; UniProt 2–439

Tubulin beta-2B chain

OrganismNot specified

UniProt Q6B856

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 5 Calmodulin-regulated spectrin-associated protein 1 × 1 (Q5T5Y3) Tubulin alpha chain × 2 (F2Z4C1) GUANOSINE-5'-TRIPHOSPHATE × 2 MAGNESIUM ION × 2 GUANOSINE-5'-DIPHOSPHATE × 2 TAXOL × 2 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name TBB2B_BOVIN
Isoform —
PDB entities 3
Chains and sequence ranges Author chain B; PDBConstruct 1–426; UniProt 2–427 Author chain E; PDBConstruct 1–426; UniProt 2–427

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_id5m5c
Deposition date deposition_date2016-10-21
Structure title titleMechanism of microtubule minus-end recognition and protection by CAMSAP proteins
Keywords keywordsCAMSAP CKK Microtubule Tubulin, TRANSPORT PROTEIN; TRANSPORT PROTEIN
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.

5m5c__assembly_1__model_1

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

Download this curve (.dat)

5m5c__assembly_1__model_1 | I(q)

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

5m5c__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)40.00 Å
Rg (electron density)39.49 Å
Total Rg39.82 Å
Atom count14600
Residues1826
Excluded volume257940 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 5m5c__assembly_1__model_1 pentameric (5) 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 (8)

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7. Citations (1)