7x0s

Human TRiC-tubulin-S3

Method: ELECTRON MICROSCOPY Dmax: 163.7 Å Quality: GOOD

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

T-complex protein 1 subunit zeta

Homo sapiens

UniProt P40227

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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain K; UniProt 1–531 Chain z; UniProt 1–531 Not recorded T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit alpha × 2 (P17987) Tubulin beta chain × 1 (P07437) ADP ADENOSINE-5'-DIPHOSPHATE × 16 MG MAGNESIUM ION × 16 AF3 ALUMINUM FLUORIDE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

64 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TCPZ_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain K; PDBConstruct 1–531; UniProt 1–531 Author chain z; PDBConstruct 1–531; UniProt 1–531

T-complex protein 1 subunit theta

Homo sapiens

UniProt P50990

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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain J; UniProt 1–548 Chain P; UniProt 1–548 Not recorded T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit alpha × 2 (P17987) Tubulin beta chain × 1 (P07437) ADP ADENOSINE-5'-DIPHOSPHATE × 16 MG MAGNESIUM ION × 16 AF3 ALUMINUM FLUORIDE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

64 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TCPQ_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain J; PDBConstruct 1–548; UniProt 1–548 Author chain P; PDBConstruct 1–548; UniProt 1–548

T-complex protein 1 subunit eta

Homo sapiens

UniProt Q99832

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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain H; UniProt 1–543 Chain O; UniProt 1–543 Mutation:L290S T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit alpha × 2 (P17987) Tubulin beta chain × 1 (P07437) ADP ADENOSINE-5'-DIPHOSPHATE × 16 MG MAGNESIUM ION × 16 AF3 ALUMINUM FLUORIDE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

63 other PDB entries and 63 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TCPH_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain H; PDBConstruct 1–543; UniProt 1–543 Author chain O; PDBConstruct 1–543; UniProt 1–543

T-complex protein 1 subunit gamma

Homo sapiens

UniProt P49368

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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain G; UniProt 1–545 Chain N; UniProt 1–545 Not recorded T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit alpha × 2 (P17987) Tubulin beta chain × 1 (P07437) ADP ADENOSINE-5'-DIPHOSPHATE × 16 MG MAGNESIUM ION × 16 AF3 ALUMINUM FLUORIDE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

65 other PDB entries and 65 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TCPG_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain G; PDBConstruct 1–545; UniProt 1–545 Author chain N; PDBConstruct 1–545; UniProt 1–545

T-complex protein 1 subunit epsilon

Homo sapiens

UniProt P48643

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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain E; UniProt 3–541 Chain e; UniProt 3–541 Not recorded T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit alpha × 2 (P17987) Tubulin beta chain × 1 (P07437) ADP ADENOSINE-5'-DIPHOSPHATE × 16 MG MAGNESIUM ION × 16 AF3 ALUMINUM FLUORIDE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

68 other PDB entries and 68 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TCPE_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–539; UniProt 3–541 Author chain e; PDBConstruct 1–539; UniProt 3–541

T-complex protein 1 subunit delta

Homo sapiens

UniProt P50991

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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain I; UniProt 1–539 Chain M; UniProt 1–539 Not recorded T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit alpha × 2 (P17987) Tubulin beta chain × 1 (P07437) ADP ADENOSINE-5'-DIPHOSPHATE × 16 MG MAGNESIUM ION × 16 AF3 ALUMINUM FLUORIDE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

65 other PDB entries and 65 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TCPD_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain I; PDBConstruct 1–539; UniProt 1–539 Author chain M; PDBConstruct 1–539; UniProt 1–539

T-complex protein 1 subunit beta

Homo sapiens

UniProt P78371

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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain B; UniProt 1–535 Chain L; UniProt 1–535 Not recorded T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit alpha × 2 (P17987) Tubulin beta chain × 1 (P07437) ADP ADENOSINE-5'-DIPHOSPHATE × 16 MG MAGNESIUM ION × 16 AF3 ALUMINUM FLUORIDE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

64 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TCPB_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain B; PDBConstruct 1–535; UniProt 1–535 Author chain L; PDBConstruct 1–535; UniProt 1–535

T-complex protein 1 subunit alpha

Homo sapiens

UniProt P17987

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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain A; UniProt 1–556 Chain a; UniProt 1–556 Not recorded T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit beta × 2 (P78371) Tubulin beta chain × 1 (P07437) ADP ADENOSINE-5'-DIPHOSPHATE × 16 MG MAGNESIUM ION × 16 AF3 ALUMINUM FLUORIDE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

64 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TCPA_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain A; PDBConstruct 1–556; UniProt 1–556 Author chain a; PDBConstruct 1–556; UniProt 1–556

Tubulin beta chain

Homo sapiens

UniProt P07437

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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain R; UniProt 1–444 Not recorded T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit alpha × 2 (P17987) ADP ADENOSINE-5'-DIPHOSPHATE × 16 MG MAGNESIUM ION × 16 AF3 ALUMINUM FLUORIDE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBB5_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain R; PDBConstruct 1–444; UniProt 1–444

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 7x0s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7x0s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7x0s
Deposition date deposition_date2022-02-22
Structure title titleHuman TRiC-tubulin-S3
Keywords keywordsSTRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier64.87
Radius of gyration Rg (electron density) rg_electron63.81
Forward intensity I(0) i013417500000.00
Molecular weight molecular_weight977540.0 kDa
Excluded volume excluded_volume1223700 ų
Envelope volume envelope_volume1897600 ų
Hydration-shell volume shell_volume229710 ų
Envelope diameter envelope_diameter181.5
Shell Rg shell_rg79.07
Envelope Rg envelope_rg60.38
Shape Rg shape_rg63.82
Total Rg total_rg64.00
Total atoms total_atoms68330
Residues n_residues8866
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 dmax163.7
Rg (real space) rg_real64.05
Rg uncertainty (real space) rg_real_error0.52
I(0) (real space) i0_real1.3420e+10
I(0) uncertainty (real space) i0_real_error2.3130e+08
Rg (reciprocal space) rg_reciprocal65.55
I(0) (reciprocal space) i0_reciprocal13450000000.0000
Solution quality estimate total_estimate0.8448
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary95.5
Skewness Skewness skewness-0.182
Kurtosis Kurtosis kurtosis-0.646
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4311000000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.993; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (13)

7. Fold Classification (SCOP + CATH) 11 domains

CATH v4.4 (11 domains)

Domain ID domain_id7x0sA01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology7 — GroEL
Homologous superfamily homologous superfamily10 — GroEL
Domain ID domain_id7x0sB01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology7 — GroEL
Homologous superfamily homologous superfamily10 — GroEL
Domain ID domain_id7x0sH01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology7 — GroEL
Homologous superfamily homologous superfamily10 — GroEL
Domain ID domain_id7x0sJ01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology7 — GroEL
Homologous superfamily homologous superfamily10 — GroEL
Domain ID domain_id7x0sL01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology7 — GroEL
Homologous superfamily homologous superfamily10 — GroEL
Domain ID domain_id7x0sO01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology7 — GroEL
Homologous superfamily homologous superfamily10 — GroEL
Domain ID domain_id7x0sP01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology7 — GroEL
Homologous superfamily homologous superfamily10 — GroEL
Domain ID domain_id7x0sR01
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_id7x0sR02
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_id7x0sR03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily600 — Helix hairpin bin
Domain ID domain_id7x0sa01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology7 — GroEL
Homologous superfamily homologous superfamily10 — GroEL

8. Citations (1)

9. Files and Curves (10)