8r67

tubulin-cryptophycin complex

Method: X-RAY DIFFRACTION Dmax: 184.3 Å Quality: REASONABLE

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

Detyrosinated tubulin alpha-1B chain

OrganismNot specified

UniProt P81947

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–451 Chain C; UniProt 1–451 Not recorded Tubulin beta-2B chain × 2 (Q6B856) Stathmin-4 × 1 (P63043) Tubulin tyrosine ligase × 1 (A0A8V0Z8P0) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 5 CA CALCIUM ION × 4 GDP GUANOSINE-5'-DIPHOSPHATE × 2 IMD IMIDAZOLE × 5 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 GOL GLYCEROL × 1 Y74 2-[(3~{S},10~{R},13~{E},16~{S})-10-[(3-chloranyl-4-methoxy-phenyl)methyl]-6,6-dimethyl-2,5,9,12-tetrakis(oxidanylidene)-16-[(1~{S})-1-[(2~{R},3~{R})-3-phenyloxiran-2-yl]ethyl]-1,4-dioxa-8,11-diazacyclohexadec-13-en-3-yl]ethanoic acid × 2 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;5% PEG 4K, 8% glycerol, 30 mM MgCl2, 30 mM CaCl2, 0.1 M MES/Imidazole, 5 mM L-tyrosine Resolution 2.20 Å R-free 0.229

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.

249 other PDB entries and 251 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBA1B_BOVIN
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-2B chain

OrganismNot specified

UniProt Q6B856

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 1–445 Chain D; UniProt 1–445 Not recorded Detyrosinated tubulin alpha-1B chain × 2 (P81947) Stathmin-4 × 1 (P63043) Tubulin tyrosine ligase × 1 (A0A8V0Z8P0) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 5 CA CALCIUM ION × 4 GDP GUANOSINE-5'-DIPHOSPHATE × 2 IMD IMIDAZOLE × 5 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 GOL GLYCEROL × 1 Y74 2-[(3~{S},10~{R},13~{E},16~{S})-10-[(3-chloranyl-4-methoxy-phenyl)methyl]-6,6-dimethyl-2,5,9,12-tetrakis(oxidanylidene)-16-[(1~{S})-1-[(2~{R},3~{R})-3-phenyloxiran-2-yl]ethyl]-1,4-dioxa-8,11-diazacyclohexadec-13-en-3-yl]ethanoic acid × 2 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;5% PEG 4K, 8% glycerol, 30 mM MgCl2, 30 mM CaCl2, 0.1 M MES/Imidazole, 5 mM L-tyrosine Resolution 2.20 Å R-free 0.229

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.

273 other PDB entries and 275 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBB2B_BOVIN
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

Stathmin-4

Rattus norvegicus

UniProt P63043

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain E; UniProt 49–189 Not recorded Detyrosinated tubulin alpha-1B chain × 2 (P81947) Tubulin beta-2B chain × 2 (Q6B856) Tubulin tyrosine ligase × 1 (A0A8V0Z8P0) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 5 CA CALCIUM ION × 4 GDP GUANOSINE-5'-DIPHOSPHATE × 2 IMD IMIDAZOLE × 5 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 GOL GLYCEROL × 1 Y74 2-[(3~{S},10~{R},13~{E},16~{S})-10-[(3-chloranyl-4-methoxy-phenyl)methyl]-6,6-dimethyl-2,5,9,12-tetrakis(oxidanylidene)-16-[(1~{S})-1-[(2~{R},3~{R})-3-phenyloxiran-2-yl]ethyl]-1,4-dioxa-8,11-diazacyclohexadec-13-en-3-yl]ethanoic acid × 2 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;5% PEG 4K, 8% glycerol, 30 mM MgCl2, 30 mM CaCl2, 0.1 M MES/Imidazole, 5 mM L-tyrosine Resolution 2.20 Å R-free 0.229

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.

287 other PDB entries and 287 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name STMN4_RAT
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 3–143; UniProt 49–189

Tubulin tyrosine ligase

Gallus gallus

UniProt A0A8V0Z8P0

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain F; UniProt 1–52 Chain F; UniProt 86–411 Not recorded Detyrosinated tubulin alpha-1B chain × 2 (P81947) Tubulin beta-2B chain × 2 (Q6B856) Stathmin-4 × 1 (P63043) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 5 CA CALCIUM ION × 4 GDP GUANOSINE-5'-DIPHOSPHATE × 2 IMD IMIDAZOLE × 5 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 GOL GLYCEROL × 1 Y74 2-[(3~{S},10~{R},13~{E},16~{S})-10-[(3-chloranyl-4-methoxy-phenyl)methyl]-6,6-dimethyl-2,5,9,12-tetrakis(oxidanylidene)-16-[(1~{S})-1-[(2~{R},3~{R})-3-phenyloxiran-2-yl]ethyl]-1,4-dioxa-8,11-diazacyclohexadec-13-en-3-yl]ethanoic acid × 2 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;5% PEG 4K, 8% glycerol, 30 mM MgCl2, 30 mM CaCl2, 0.1 M MES/Imidazole, 5 mM L-tyrosine Resolution 2.20 Å R-free 0.229

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.

25 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8V0Z8P0_CHICK
Isoform
PDB entities 4
Chains and sequence ranges Author chain F; PDBConstruct 1–52; UniProt 1–52 Author chain F; PDBConstruct 53–378; UniProt 86–411

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 8r67

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8r67
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8r67
Deposition date deposition_date2023-11-21
Structure title titletubulin-cryptophycin complex
Keywords keywordsCELL CYCLE, TUBULIN FOLD, CYTOSKELETON, MICROTUBULE; CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier56.27
Radius of gyration Rg (electron density) rg_electron57.29
Forward intensity I(0) i0945434000.00
Molecular weight molecular_weight250900.0 kDa
Excluded volume excluded_volume311400 ų
Envelope volume envelope_volume415950 ų
Hydration-shell volume shell_volume66566 ų
Envelope diameter envelope_diameter202.1
Shell Rg shell_rg50.50
Envelope Rg envelope_rg57.37
Shape Rg shape_rg57.30
Total Rg total_rg57.06
Total atoms total_atoms17599
Residues n_residues2184
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 dmax184.3
Rg (real space) rg_real57.04
Rg uncertainty (real space) rg_real_error1.97
I(0) (real space) i0_real9.4540e+08
I(0) uncertainty (real space) i0_real_error1.6530e+07
Rg (reciprocal space) rg_reciprocal55.60
I(0) (reciprocal space) i0_reciprocal943400000.0000
Solution quality estimate total_estimate0.7165
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.5
Skewness Skewness skewness0.560
Kurtosis Kurtosis kurtosis-0.552
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha87890000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.575; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.580; Smooth: 0.006

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (14)

8. Citations (1)

9. Files and Curves (10)