1z5w

Crystal Structure of gamma-tubulin bound to GTP

Method: X-RAY DIFFRACTION Dmax: 71.6 Å Quality: GOOD

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

Tubulin gamma-1 chain

Homo sapiens

UniProt P23258

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–449 Not recorded MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 8.2;277 K;Tris, KCl, PEG6000, pH 8.2, VAPOR DIFFUSION, temperature 277K Resolution 3.00 Å R-free 0.309

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.

31 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBG1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–449; UniProt 1–449

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 1z5w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1z5w
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1z5w
Deposition date deposition_date2005-03-20
Structure title titleCrystal Structure of gamma-tubulin bound to GTP
Keywords keywordscomplex with GTP, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.03
Radius of gyration Rg (electron density) rg_electron20.78
Forward intensity I(0) i034280000.00
Molecular weight molecular_weight44192.0 kDa
Excluded volume excluded_volume54907 ų
Envelope volume envelope_volume65040 ų
Hydration-shell volume shell_volume25312 ų
Envelope diameter envelope_diameter73.2
Shell Rg shell_rg28.27
Envelope Rg envelope_rg21.27
Shape Rg shape_rg20.81
Total Rg total_rg21.60
Total atoms total_atoms3110
Residues n_residues409
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 dmax71.6
Rg (real space) rg_real21.89
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real3.4280e+07
I(0) uncertainty (real space) i0_real_error4.1790e+05
Rg (reciprocal space) rg_reciprocal21.92
I(0) (reciprocal space) i0_reciprocal34280000.0000
Solution quality estimate total_estimate0.8872
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.8
Skewness Skewness skewness0.194
Kurtosis Kurtosis kurtosis-0.367
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8567000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.843; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1z5wa1
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.32.1.0 — automated matches
Domain ID domain_idd1z5wa2
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.79.2.0 — automated matches

CATH v4.4 (3 domains)

Domain ID domain_id1z5wA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1440 — Tubulin/FtsZ, GTPase domain
Domain ID domain_id1z5wA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily20 — Tubulin/FtsZ, C-terminal domain
Domain ID domain_id1z5wA03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily600 — Helix hairpin bin

8. Citations (1)

9. Files and Curves (10)