6y4n

Structure of Tubulin Tyrosine Ligase in Complex with Tb116

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

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–451 Chain C; UniProt 1–451 Not recorded Tubulin beta chain × 2 (P02554) Stathmin-4 × 1 (P63043) Tubulin-Tyrosine Ligase × 1 (E1BQ43) GTP GUANOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 CA CALCIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 O9B (2~{R})-1-methylpiperidine-2-carboxylic acid × 1 O9K [(1~{R},3~{R})-1-(4-methanoyl-1,3-thiazol-2-yl)-4-methyl-3-(methylamino)pentyl] ethanoate × 1 O9N methyl (2~{S},4~{S})-2,4-bis(azanyl)-5-phenyl-pentanoate × 1 PGE TRIETHYLENE GLYCOL × 1 VAL VALINE × 1 P6S benzyl hydrogen carbonate × 1 PEG DI(HYDROXYETHYL)ETHER × 1 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;293 K;30 mM calcium chloride, 30 mM magnesium chloride, 0.10 M MES pH 6.0, 2.0% w/v PEG 4000, 5.0% w/v glycerol Resolution 2.85 Å R-free 0.220

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 1–445 Chain D; UniProt 1–445 Not recorded Tubulin alpha-1B chain × 2 (Q2XVP4) Stathmin-4 × 1 (P63043) Tubulin-Tyrosine Ligase × 1 (E1BQ43) GTP GUANOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 CA CALCIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 O9B (2~{R})-1-methylpiperidine-2-carboxylic acid × 1 O9K [(1~{R},3~{R})-1-(4-methanoyl-1,3-thiazol-2-yl)-4-methyl-3-(methylamino)pentyl] ethanoate × 1 O9N methyl (2~{S},4~{S})-2,4-bis(azanyl)-5-phenyl-pentanoate × 1 PGE TRIETHYLENE GLYCOL × 1 VAL VALINE × 1 P6S benzyl hydrogen carbonate × 1 PEG DI(HYDROXYETHYL)ETHER × 1 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;293 K;30 mM calcium chloride, 30 mM magnesium chloride, 0.10 M MES pH 6.0, 2.0% w/v PEG 4000, 5.0% w/v glycerol Resolution 2.85 Å R-free 0.220

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

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 Tubulin alpha-1B chain × 2 (Q2XVP4) Tubulin beta chain × 2 (P02554) Tubulin-Tyrosine Ligase × 1 (E1BQ43) GTP GUANOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 CA CALCIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 O9B (2~{R})-1-methylpiperidine-2-carboxylic acid × 1 O9K [(1~{R},3~{R})-1-(4-methanoyl-1,3-thiazol-2-yl)-4-methyl-3-(methylamino)pentyl] ethanoate × 1 O9N methyl (2~{S},4~{S})-2,4-bis(azanyl)-5-phenyl-pentanoate × 1 PGE TRIETHYLENE GLYCOL × 1 VAL VALINE × 1 P6S benzyl hydrogen carbonate × 1 PEG DI(HYDROXYETHYL)ETHER × 1 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;293 K;30 mM calcium chloride, 30 mM magnesium chloride, 0.10 M MES pH 6.0, 2.0% w/v PEG 4000, 5.0% w/v glycerol Resolution 2.85 Å R-free 0.220

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 E1BQ43

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 1–378 Not recorded Tubulin alpha-1B chain × 2 (Q2XVP4) Tubulin beta chain × 2 (P02554) Stathmin-4 × 1 (P63043) GTP GUANOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 CA CALCIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 O9B (2~{R})-1-methylpiperidine-2-carboxylic acid × 1 O9K [(1~{R},3~{R})-1-(4-methanoyl-1,3-thiazol-2-yl)-4-methyl-3-(methylamino)pentyl] ethanoate × 1 O9N methyl (2~{S},4~{S})-2,4-bis(azanyl)-5-phenyl-pentanoate × 1 PGE TRIETHYLENE GLYCOL × 1 VAL VALINE × 1 P6S benzyl hydrogen carbonate × 1 PEG DI(HYDROXYETHYL)ETHER × 1 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;293 K;30 mM calcium chloride, 30 mM magnesium chloride, 0.10 M MES pH 6.0, 2.0% w/v PEG 4000, 5.0% w/v glycerol Resolution 2.85 Å R-free 0.220

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.

241 other PDB entries and 241 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name E1BQ43_CHICK
Isoform
PDB entities 4
Chains and sequence ranges Author chain F; PDBConstruct 1–378; UniProt 1–378

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 6y4n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6y4n
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6y4n
Deposition date deposition_date2020-02-21
Structure title titleStructure of Tubulin Tyrosine Ligase in Complex with Tb116
Keywords keywordsTTL, Tubulin, ligase, complex; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier56.19
Radius of gyration Rg (electron density) rg_electron56.99
Forward intensity I(0) i0961510000.00
Molecular weight molecular_weight252540.0 kDa
Excluded volume excluded_volume313240 ų
Envelope volume envelope_volume424730 ų
Hydration-shell volume shell_volume67637 ų
Envelope diameter envelope_diameter199.2
Shell Rg shell_rg51.03
Envelope Rg envelope_rg57.11
Shape Rg shape_rg57.00
Total Rg total_rg56.80
Total atoms total_atoms17716
Residues n_residues2207
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_real56.92
Rg uncertainty (real space) rg_real_error2.13
I(0) (real space) i0_real9.6150e+08
I(0) uncertainty (real space) i0_real_error1.8890e+07
Rg (reciprocal space) rg_reciprocal55.54
I(0) (reciprocal space) i0_reciprocal959500000.0000
Solution quality estimate total_estimate0.5042
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.5
Skewness Skewness skewness0.548
Kurtosis Kurtosis kurtosis-0.576
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha93170000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.610; Stabil: 0.999; Sysdev: 0.041; Positv: 1.000; Valcen: 0.592; Smooth: 0.007

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (18)

7. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (12 domains)

Domain ID domain_idd6y4na1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.32 — Tubulin nucleotide-binding domain-like
Superfamily Superfamily superfamilyc.32.1 — Tubulin nucleotide-binding domain-like
Family Family familyc.32.1.1 — Tubulin, GTPase domain
Domain ID domain_idd6y4na2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.79 — Bacillus chorismate mutase-like
Superfamily Superfamily superfamilyd.79.2 — Tubulin C-terminal domain-like
Family Family familyd.79.2.1 — Tubulin, C-terminal domain
Domain ID domain_idd6y4nb1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.32 — Tubulin nucleotide-binding domain-like
Superfamily Superfamily superfamilyc.32.1 — Tubulin nucleotide-binding domain-like
Family Family familyc.32.1.1 — Tubulin, GTPase domain
Domain ID domain_idd6y4nb2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.79 — Bacillus chorismate mutase-like
Superfamily Superfamily superfamilyd.79.2 — Tubulin C-terminal domain-like
Family Family familyd.79.2.1 — Tubulin, C-terminal domain
Domain ID domain_idd6y4nc1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.32 — Tubulin nucleotide-binding domain-like
Superfamily Superfamily superfamilyc.32.1 — Tubulin nucleotide-binding domain-like
Family Family familyc.32.1.1 — Tubulin, GTPase domain
Domain ID domain_idd6y4nc2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.79 — Bacillus chorismate mutase-like
Superfamily Superfamily superfamilyd.79.2 — Tubulin C-terminal domain-like
Family Family familyd.79.2.1 — Tubulin, C-terminal domain
Domain ID domain_idd6y4nd1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.32 — Tubulin nucleotide-binding domain-like
Superfamily Superfamily superfamilyc.32.1 — Tubulin nucleotide-binding domain-like
Family Family familyc.32.1.1 — Tubulin, GTPase domain
Domain ID domain_idd6y4nd2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.79 — Bacillus chorismate mutase-like
Superfamily Superfamily superfamilyd.79.2 — Tubulin C-terminal domain-like
Family Family familyd.79.2.1 — Tubulin, C-terminal domain
Domain ID domain_idd6y4ne_
Class classa — All alpha proteins
Fold Fold folda.137 — Non-globular all-alpha subunits of globular proteins
Superfamily Superfamily superfamilya.137.10 — Stathmin
Family Family familya.137.10.1 — Stathmin
Domain ID domain_idd6y4nf1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.30 — PreATP-grasp domain
Superfamily Superfamily superfamilyc.30.1 — PreATP-grasp domain
Family Family familyc.30.1.9 — Tubulin tyrosine ligase (TTL) N-terminal domain-like
Domain ID domain_idd6y4nf2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.142 — ATP-grasp
Superfamily Superfamily superfamilyd.142.1 — Glutathione synthetase ATP-binding domain-like
Family Family familyd.142.1.10 — Tubulin tyrosine ligase (TTL) C-terminal domain-like
Domain ID domain_idd6y4nf3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id6y4nF01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily11480
Domain ID domain_id6y4nF02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology470 — D-amino Acid Aminotransferase; Chain A, domain 1
Homologous superfamily homologous superfamily20 — ATP-grasp fold, B domain

8. Citations (1)

9. Files and Curves (10)