6nrb

hTRiC-hPFD Class2

Method: ELECTRON MICROSCOPY Dmax: 272.2 Å Quality: GOOD

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

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain A; UniProt 1–534 Chain I; UniProt 1–534 Not recorded T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit theta × 2 (P50990) Prefoldin subunit 1 × 1 (O60925) Prefoldin subunit 2 × 1 (Q9UHV9) Prefoldin subunit 3 × 1 (P61758) Prefoldin subunit 4 × 1 (Q9NQP4) Prefoldin subunit 5 × 1 (Q99471) Prefoldin subunit 6 × 1 (O15212) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.70 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 1–534; UniProt 1–534 Author chain I; PDBConstruct 1–534; UniProt 1–534

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain B; UniProt 16–524 Chain J; UniProt 16–524 Not recorded T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit theta × 2 (P50990) Prefoldin subunit 1 × 1 (O60925) Prefoldin subunit 2 × 1 (Q9UHV9) Prefoldin subunit 3 × 1 (P61758) Prefoldin subunit 4 × 1 (Q9NQP4) Prefoldin subunit 5 × 1 (Q99471) Prefoldin subunit 6 × 1 (O15212) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.70 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 1–509; UniProt 16–524 Author chain J; PDBConstruct 1–509; UniProt 16–524

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain C; UniProt 13–525 Chain K; UniProt 13–525 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 zeta × 2 (P40227) T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit theta × 2 (P50990) Prefoldin subunit 1 × 1 (O60925) Prefoldin subunit 2 × 1 (Q9UHV9) Prefoldin subunit 3 × 1 (P61758) Prefoldin subunit 4 × 1 (Q9NQP4) Prefoldin subunit 5 × 1 (Q99471) Prefoldin subunit 6 × 1 (O15212) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.70 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 3
Chains and sequence ranges Author chain C; PDBConstruct 1–513; UniProt 13–525 Author chain K; PDBConstruct 1–513; UniProt 13–525

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain D; UniProt 26–539 Chain L; UniProt 26–539 Not recorded T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit theta × 2 (P50990) Prefoldin subunit 1 × 1 (O60925) Prefoldin subunit 2 × 1 (Q9UHV9) Prefoldin subunit 3 × 1 (P61758) Prefoldin subunit 4 × 1 (Q9NQP4) Prefoldin subunit 5 × 1 (Q99471) Prefoldin subunit 6 × 1 (O15212) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.70 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 4
Chains and sequence ranges Author chain D; PDBConstruct 1–514; UniProt 26–539 Author chain L; PDBConstruct 1–514; UniProt 26–539

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain E; UniProt 25–541 Chain M; UniProt 25–541 Not recorded T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit theta × 2 (P50990) Prefoldin subunit 1 × 1 (O60925) Prefoldin subunit 2 × 1 (Q9UHV9) Prefoldin subunit 3 × 1 (P61758) Prefoldin subunit 4 × 1 (Q9NQP4) Prefoldin subunit 5 × 1 (Q99471) Prefoldin subunit 6 × 1 (O15212) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.70 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 1–517; UniProt 25–541 Author chain M; PDBConstruct 1–517; UniProt 25–541

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain F; UniProt 11–525 Chain N; UniProt 11–525 Not recorded T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit theta × 2 (P50990) Prefoldin subunit 1 × 1 (O60925) Prefoldin subunit 2 × 1 (Q9UHV9) Prefoldin subunit 3 × 1 (P61758) Prefoldin subunit 4 × 1 (Q9NQP4) Prefoldin subunit 5 × 1 (Q99471) Prefoldin subunit 6 × 1 (O15212) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.70 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 6
Chains and sequence ranges Author chain F; PDBConstruct 1–515; UniProt 11–525 Author chain N; PDBConstruct 1–515; UniProt 11–525

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain G; UniProt 12–525 Chain O; UniProt 12–525 Not recorded T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit theta × 2 (P50990) Prefoldin subunit 1 × 1 (O60925) Prefoldin subunit 2 × 1 (Q9UHV9) Prefoldin subunit 3 × 1 (P61758) Prefoldin subunit 4 × 1 (Q9NQP4) Prefoldin subunit 5 × 1 (Q99471) Prefoldin subunit 6 × 1 (O15212) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.70 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 7
Chains and sequence ranges Author chain G; PDBConstruct 1–514; UniProt 12–525 Author chain O; PDBConstruct 1–514; UniProt 12–525

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain H; UniProt 14–527 Chain P; UniProt 14–527 Not recorded T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit eta × 2 (Q99832) Prefoldin subunit 1 × 1 (O60925) Prefoldin subunit 2 × 1 (Q9UHV9) Prefoldin subunit 3 × 1 (P61758) Prefoldin subunit 4 × 1 (Q9NQP4) Prefoldin subunit 5 × 1 (Q99471) Prefoldin subunit 6 × 1 (O15212) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.70 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 H; PDBConstruct 1–514; UniProt 14–527 Author chain P; PDBConstruct 1–514; UniProt 14–527

Prefoldin subunit 1

Homo sapiens

UniProt O60925

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain 1; UniProt 12–118 Not recorded T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit theta × 2 (P50990) Prefoldin subunit 2 × 1 (Q9UHV9) Prefoldin subunit 3 × 1 (P61758) Prefoldin subunit 4 × 1 (Q9NQP4) Prefoldin subunit 5 × 1 (Q99471) Prefoldin subunit 6 × 1 (O15212) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.70 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PFD1_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain 1; PDBConstruct 1–107; UniProt 12–118

Prefoldin subunit 2

Homo sapiens

UniProt Q9UHV9

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain 2; UniProt 22–124 Not recorded T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit theta × 2 (P50990) Prefoldin subunit 1 × 1 (O60925) Prefoldin subunit 3 × 1 (P61758) Prefoldin subunit 4 × 1 (Q9NQP4) Prefoldin subunit 5 × 1 (Q99471) Prefoldin subunit 6 × 1 (O15212) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.70 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PFD2_HUMAN
Isoform
PDB entities 10
Chains and sequence ranges Author chain 2; PDBConstruct 1–103; UniProt 22–124

Prefoldin subunit 3

Homo sapiens

UniProt P61758

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain 3; UniProt 49–180 Not recorded T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit theta × 2 (P50990) Prefoldin subunit 1 × 1 (O60925) Prefoldin subunit 2 × 1 (Q9UHV9) Prefoldin subunit 4 × 1 (Q9NQP4) Prefoldin subunit 5 × 1 (Q99471) Prefoldin subunit 6 × 1 (O15212) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.70 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PFD3_HUMAN
Isoform
PDB entities 11
Chains and sequence ranges Author chain 3; PDBConstruct 1–132; UniProt 49–180

Prefoldin subunit 4

Homo sapiens

UniProt Q9NQP4

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain 4; UniProt 19–122 Not recorded T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit theta × 2 (P50990) Prefoldin subunit 1 × 1 (O60925) Prefoldin subunit 2 × 1 (Q9UHV9) Prefoldin subunit 3 × 1 (P61758) Prefoldin subunit 5 × 1 (Q99471) Prefoldin subunit 6 × 1 (O15212) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.70 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PFD4_HUMAN
Isoform
PDB entities 12
Chains and sequence ranges Author chain 4; PDBConstruct 1–104; UniProt 19–122

Prefoldin subunit 5

Homo sapiens

UniProt Q99471

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain 5; UniProt 11–137 Not recorded T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit theta × 2 (P50990) Prefoldin subunit 1 × 1 (O60925) Prefoldin subunit 2 × 1 (Q9UHV9) Prefoldin subunit 3 × 1 (P61758) Prefoldin subunit 4 × 1 (Q9NQP4) Prefoldin subunit 6 × 1 (O15212) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.70 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PFD5_HUMAN
Isoform
PDB entities 13
Chains and sequence ranges Author chain 5; PDBConstruct 1–127; UniProt 11–137

Prefoldin subunit 6

Homo sapiens

UniProt O15212

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain 6; UniProt 13–114 Not recorded T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit theta × 2 (P50990) Prefoldin subunit 1 × 1 (O60925) Prefoldin subunit 2 × 1 (Q9UHV9) Prefoldin subunit 3 × 1 (P61758) Prefoldin subunit 4 × 1 (Q9NQP4) Prefoldin subunit 5 × 1 (Q99471) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.70 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PFD6_HUMAN
Isoform
PDB entities 14
Chains and sequence ranges Author chain 6; PDBConstruct 1–102; UniProt 13–114

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 6nrb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6nrb
Deposition date deposition_date2019-01-23
Structure title titlehTRiC-hPFD Class2
Keywords keywordsTRiC/CCT, PFD, CryoEM, Molecular Chaperone, Protein folding, CHAPERONE; CHAPERONE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier75.25
Radius of gyration Rg (electron density) rg_electron74.80
Forward intensity I(0) i013117300000.00
Molecular weight molecular_weight975930.0 kDa
Excluded volume excluded_volume1225500 ų
Envelope volume envelope_volume2144000 ų
Hydration-shell volume shell_volume234500 ų
Envelope diameter envelope_diameter249.0
Shell Rg shell_rg83.51
Envelope Rg envelope_rg69.80
Shape Rg shape_rg74.81
Total Rg total_rg74.88
Total atoms total_atoms68284
Residues n_residues8896
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 dmax272.2
Rg (real space) rg_real77.55
Rg uncertainty (real space) rg_real_error1.66
I(0) (real space) i0_real1.3120e+10
I(0) uncertainty (real space) i0_real_error2.7160e+08
Rg (reciprocal space) rg_reciprocal76.53
I(0) (reciprocal space) i0_reciprocal13160000000.0000
Solution quality estimate total_estimate0.8205
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary103.7
Skewness Skewness skewness0.426
Kurtosis Kurtosis kurtosis0.655
Angular range angular_range— – 0.1050 −1
Current regularization parameter α current_alpha0.7338
Highest regularization parameter α highest_alpha2705000000.0000
Real-space data points n_real_points22
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.400; Stabil: 0.932; Sysdev: 1.000; Positv: 1.000; Valcen: 0.939; Smooth: 0.952

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (14)

8. Citations (1)

9. Files and Curves (10)