8v4m

CCP5 in complex with microtubules class3

Method: ELECTRON MICROSCOPY Dmax: 131.1 Å Quality: GOOD

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

Tubulin alpha-1B chain

OrganismNot specified

UniProt Q2XVP4

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 5 PDB declaration: hexameric(6) Count mismatch; review required Chain A; UniProt 1–451 Chain C; UniProt 1–451 Not recorded Tubulin beta chain × 2 (P02554) Cytosolic carboxypeptidase-like protein 5 × 1 (Q8NDL9) MG MAGNESIUM ION × 4 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 2 GLU GLUTAMIC ACID × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

230 other PDB entries and 243 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBA1B_PIG
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–451; UniProt 1–451 Author chain C; PDBConstruct 1–451; UniProt 1–451

Tubulin beta chain

OrganismNot specified

UniProt P02554

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 5 PDB declaration: hexameric(6) Count mismatch; review required Chain B; UniProt 1–445 Chain D; UniProt 1–445 Not recorded Tubulin alpha-1B chain × 2 (Q2XVP4) Cytosolic carboxypeptidase-like protein 5 × 1 (Q8NDL9) MG MAGNESIUM ION × 4 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 2 GLU GLUTAMIC ACID × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

137 other PDB entries and 159 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBB_PIG
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–445; UniProt 1–445 Author chain D; PDBConstruct 1–445; UniProt 1–445

Cytosolic carboxypeptidase-like protein 5

Homo sapiens

UniProt Q8NDL9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 5 PDB declaration: hexameric(6) Count mismatch; review required Chain E; UniProt 2–605 Fragment:residues 2-605 Mutation:E516A Tubulin alpha-1B chain × 2 (Q2XVP4) Tubulin beta chain × 2 (P02554) MG MAGNESIUM ION × 4 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 2 GLU GLUTAMIC ACID × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CBPC5_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 2–605; UniProt 2–605

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.

SAXS scattering curve SAXS Profile

SAXS profile for 8v4m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8v4m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8v4m
Deposition date deposition_date2023-11-29
Structure title titleCCP5 in complex with microtubules class3
Keywords keywords;carboxypeptidase deglutamylation branch glutamate removal microtubule, HYDROLASE, HYDROLASE-SUBSTRATE complex, HYDROLASE-SUBSTRATE, STRUCTURAL PROTEIN complex ;; HYDROLASE/SUBSTRATE,STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier42.28
Radius of gyration Rg (electron density) rg_electron41.68
Forward intensity I(0) i0951052000.00
Molecular weight molecular_weight248080.0 kDa
Excluded volume excluded_volume307260 ų
Envelope volume envelope_volume395540 ų
Hydration-shell volume shell_volume76068 ų
Envelope diameter envelope_diameter137.3
Shell Rg shell_rg49.40
Envelope Rg envelope_rg41.11
Shape Rg shape_rg41.69
Total Rg total_rg41.95
Total atoms total_atoms17431
Residues n_residues2230
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax131.1
Rg (real space) rg_real42.04
Rg uncertainty (real space) rg_real_error1.10
I(0) (real space) i0_real9.5110e+08
I(0) uncertainty (real space) i0_real_error1.7710e+07
Rg (reciprocal space) rg_reciprocal42.28
I(0) (reciprocal space) i0_reciprocal951300000.0000
Solution quality estimate total_estimate0.8951
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary60.2
Skewness Skewness skewness0.044
Kurtosis Kurtosis kurtosis-0.587
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha241700000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.918; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.901

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)