7nvl

Human TRiC complex in closed state with nanobody bound (Consensus Map)

Method: ELECTRON MICROSCOPY Dmax: 198.7 Å Quality: GOOD

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

T-complex protein 1 subunit alpha

OrganismNot specified

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain A; UniProt 1–556 Chain a; UniProt 1–556 Not recorded T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit eta × 2 (Q99832) Nanobody Nb18 × 2 T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit zeta × 2 (P40227) 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 2.50 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–556; UniProt 1–556 Author chain a; PDBConstruct 1–556; UniProt 1–556

T-complex protein 1 subunit beta

OrganismNot specified

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain B; UniProt 1–535 Chain b; UniProt 1–535 Not recorded T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit eta × 2 (Q99832) Nanobody Nb18 × 2 T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit zeta × 2 (P40227) 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 2.50 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–535; UniProt 1–535 Author chain b; PDBConstruct 1–535; UniProt 1–535

T-complex protein 1 subunit delta

OrganismNot specified

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain D; UniProt 1–539 Chain d; UniProt 1–539 Not recorded T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit eta × 2 (Q99832) Nanobody Nb18 × 2 T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit zeta × 2 (P40227) 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 2.50 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 3
Chains and sequence ranges Author chain D; PDBConstruct 1–539; UniProt 1–539 Author chain d; PDBConstruct 1–539; UniProt 1–539

T-complex protein 1 subunit epsilon

OrganismNot specified

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain E; UniProt 1–541 Chain e; UniProt 1–541 Not recorded T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit eta × 2 (Q99832) Nanobody Nb18 × 2 T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit zeta × 2 (P40227) 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 2.50 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 4
Chains and sequence ranges Author chain E; PDBConstruct 1–541; UniProt 1–541 Author chain e; PDBConstruct 1–541; UniProt 1–541

T-complex protein 1 subunit gamma

OrganismNot specified

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain G; UniProt 1–545 Chain g; UniProt 1–545 Not recorded T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit eta × 2 (Q99832) Nanobody Nb18 × 2 T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit zeta × 2 (P40227) 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 2.50 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 5
Chains and sequence ranges Author chain G; PDBConstruct 1–545; UniProt 1–545 Author chain g; PDBConstruct 1–545; UniProt 1–545

T-complex protein 1 subunit eta

OrganismNot specified

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain H; UniProt 1–543 Chain h; UniProt 1–543 Not recorded T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit gamma × 2 (P49368) Nanobody Nb18 × 2 T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit zeta × 2 (P40227) 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 2.50 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 6
Chains and sequence ranges Author chain H; PDBConstruct 1–543; UniProt 1–543 Author chain h; PDBConstruct 1–543; UniProt 1–543

T-complex protein 1 subunit theta

OrganismNot specified

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain Q; UniProt 1–548 Chain q; UniProt 1–548 Not recorded T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit eta × 2 (Q99832) Nanobody Nb18 × 2 T-complex protein 1 subunit zeta × 2 (P40227) 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 2.50 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 8
Chains and sequence ranges Author chain Q; PDBConstruct 1–548; UniProt 1–548 Author chain q; PDBConstruct 1–548; UniProt 1–548

T-complex protein 1 subunit zeta

OrganismNot specified

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain Z; UniProt 1–531 Chain z; UniProt 1–531 Not recorded T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit eta × 2 (Q99832) Nanobody Nb18 × 2 T-complex protein 1 subunit theta × 2 (P50990) 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 2.50 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 9
Chains and sequence ranges Author chain Z; PDBConstruct 1–531; UniProt 1–531 Author chain z; PDBConstruct 1–531; UniProt 1–531

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 7nvl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7nvl
Deposition date deposition_date2021-03-15
Structure title titleHuman TRiC complex in closed state with nanobody bound (Consensus Map)
Keywords keywordsTRiC, CCT, ATP hydrolysis, type II chaperonin, protein folding, Structural Genomics, Structural Genomics Consortium, SGC, CHAPERONE; CHAPERONE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier66.37
Radius of gyration Rg (electron density) rg_electron65.24
Forward intensity I(0) i012670900000.00
Molecular weight molecular_weight950410.0 kDa
Excluded volume excluded_volume1190200 ų
Envelope volume envelope_volume1856800 ų
Hydration-shell volume shell_volume225500 ų
Envelope diameter envelope_diameter204.4
Shell Rg shell_rg78.40
Envelope Rg envelope_rg60.72
Shape Rg shape_rg65.27
Total Rg total_rg65.32
Total atoms total_atoms66434
Residues n_residues8626
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 dmax198.7
Rg (real space) rg_real65.50
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real1.2670e+10
I(0) uncertainty (real space) i0_real_error2.3120e+08
Rg (reciprocal space) rg_reciprocal67.09
I(0) (reciprocal space) i0_reciprocal12710000000.0000
Solution quality estimate total_estimate0.8599
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary99.3
Skewness Skewness skewness-0.176
Kurtosis Kurtosis kurtosis-0.544
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4025000000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.794; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.912; Smooth: 0.880

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (13)

7. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id7nvlA01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology7 — GroEL
Homologous superfamily homologous superfamily10 — GroEL
Domain ID domain_id7nvlB01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology7 — GroEL
Homologous superfamily homologous superfamily10 — GroEL
Domain ID domain_id7nvlE01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology7 — GroEL
Homologous superfamily homologous superfamily10 — GroEL
Domain ID domain_id7nvlH01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology7 — GroEL
Homologous superfamily homologous superfamily10 — GroEL
Domain ID domain_id7nvlN01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7nvlQ01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology7 — GroEL
Homologous superfamily homologous superfamily10 — GroEL
Domain ID domain_id7nvla01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology7 — GroEL
Homologous superfamily homologous superfamily10 — GroEL
Domain ID domain_id7nvlb01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology7 — GroEL
Homologous superfamily homologous superfamily10 — GroEL
Domain ID domain_id7nvle01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology7 — GroEL
Homologous superfamily homologous superfamily10 — GroEL
Domain ID domain_id7nvlh01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology7 — GroEL
Homologous superfamily homologous superfamily10 — GroEL
Domain ID domain_id7nvln01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7nvlq01
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)