SAXSdb — 3iyg

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

T-complex protein 1 subunit theta

OrganismNot specified

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 × 8 PDB declaration: octameric（8） Consistent with protein copy count	Chain Q； UniProt 17–528	Not recorded	T-complex protein 1 subunit gamma × 1 （Q3T0K2） T-complex protein 1 subunit zeta × 1 （Q3MHL7） T-complex protein 1 subunit delta × 1 （Q2T9X2） T-complex protein 1 subunit beta × 1 （Q3ZBH0） T-complex protein 1 subunit × 1 T-complex protein 1 subunit alpha × 1 （Q32L40） T-complex protein 1 subunit eta × 1 （Q2NKZ1）	ELECTRON MICROSCOPY cryo-EM vitrification conditions：two-side blotting for 1 second before plunging；101 K；Cryogen ETHANE；vitrification using ethane as cryogen	Resolution 4.00 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.

Other PDB	Difference from Current Entry 3IYG	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
4B2T The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning Deposited 2012-07-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric	Chain Q 1–548（548 aa） Chain q 1–548（548 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 5.50 Å R-free 0.399
9FQR 96-nm repeat of axonemal doublet microtubules from bovine sperm Deposited 2024-06-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 1574 PDB declaration: 1574-meric	Chain Gx 1–548（548 aa） Chain Gy 1–548（548 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 342 MG MAGNESIUM ION × 345 GDP GUANOSINE-5'-DIPHOSPHATE × 345	ELECTRON MICROSCOPY cryo-EM buffer pH 7.9 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 5.00 Å
9KCF Bovine Flagellar TRiC Deposited 2024-11-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric	Chain G 1–548（548 aa） Chain O 1–548（548 aa）	Not recorded	MG MAGNESIUM ION × 6 ADP ADENOSINE-5'-DIPHOSPHATE × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TCPQ_BOVIN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain Q； PDBConstruct 1–512； UniProt 17–528

T-complex protein 1 subunit gamma

OrganismNot specified

UniProt Q3T0K2

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 × 8 PDB declaration: octameric（8） Consistent with protein copy count	Chain G； UniProt 13–527	Not recorded	T-complex protein 1 subunit theta × 1 （Q3ZCI9） T-complex protein 1 subunit zeta × 1 （Q3MHL7） T-complex protein 1 subunit delta × 1 （Q2T9X2） T-complex protein 1 subunit beta × 1 （Q3ZBH0） T-complex protein 1 subunit × 1 T-complex protein 1 subunit alpha × 1 （Q32L40） T-complex protein 1 subunit eta × 1 （Q2NKZ1）	ELECTRON MICROSCOPY cryo-EM vitrification conditions：two-side blotting for 1 second before plunging；101 K；Cryogen ETHANE；vitrification using ethane as cryogen	Resolution 4.00 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.

Other PDB	Difference from Current Entry 3IYG	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
4B2T The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning Deposited 2012-07-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric	Chain G 1–545（545 aa） Chain g 1–545（545 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 5.50 Å R-free 0.399
9FQR 96-nm repeat of axonemal doublet microtubules from bovine sperm Deposited 2024-06-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 1574 PDB declaration: 1574-meric	Chain Io 1–545（545 aa） Chain Ip 1–545（545 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 342 MG MAGNESIUM ION × 345 GDP GUANOSINE-5'-DIPHOSPHATE × 345	ELECTRON MICROSCOPY cryo-EM buffer pH 7.9 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 5.00 Å
9KCF Bovine Flagellar TRiC Deposited 2024-11-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric	Chain C 1–545（545 aa） Chain K 1–545（545 aa）	Not recorded	MG MAGNESIUM ION × 6 ADP ADENOSINE-5'-DIPHOSPHATE × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TCPG_BOVIN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain G； PDBConstruct 1–515； UniProt 13–527

T-complex protein 1 subunit zeta

OrganismNot specified

UniProt Q3MHL7

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 × 8 PDB declaration: octameric（8） Consistent with protein copy count	Chain Z； UniProt 9–525	Not recorded	T-complex protein 1 subunit theta × 1 （Q3ZCI9） T-complex protein 1 subunit gamma × 1 （Q3T0K2） T-complex protein 1 subunit delta × 1 （Q2T9X2） T-complex protein 1 subunit beta × 1 （Q3ZBH0） T-complex protein 1 subunit × 1 T-complex protein 1 subunit alpha × 1 （Q32L40） T-complex protein 1 subunit eta × 1 （Q2NKZ1）	ELECTRON MICROSCOPY cryo-EM vitrification conditions：two-side blotting for 1 second before plunging；101 K；Cryogen ETHANE；vitrification using ethane as cryogen	Resolution 4.00 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.

Other PDB	Difference from Current Entry 3IYG	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
4B2T The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning Deposited 2012-07-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric	Chain Z 1–531（531 aa） Chain z 1–531（531 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 5.50 Å R-free 0.399
9FQR 96-nm repeat of axonemal doublet microtubules from bovine sperm Deposited 2024-06-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 1574 PDB declaration: 1574-meric	Chain Gt 1–531（531 aa） Chain Gu 1–531（531 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 342 MG MAGNESIUM ION × 345 GDP GUANOSINE-5'-DIPHOSPHATE × 345	ELECTRON MICROSCOPY cryo-EM buffer pH 7.9 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 5.00 Å
9KCF Bovine Flagellar TRiC Deposited 2024-11-01	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric	Chain P 1–531（531 aa）	Not recorded	MG MAGNESIUM ION × 6 ADP ADENOSINE-5'-DIPHOSPHATE × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TCPZ_BOVIN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain Z； PDBConstruct 1–517； UniProt 9–525

T-complex protein 1 subunit delta

OrganismNot specified

UniProt Q2T9X2

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 × 8 PDB declaration: octameric（8） Consistent with protein copy count	Chain D； UniProt 25–542	Not recorded	T-complex protein 1 subunit theta × 1 （Q3ZCI9） T-complex protein 1 subunit gamma × 1 （Q3T0K2） T-complex protein 1 subunit zeta × 1 （Q3MHL7） T-complex protein 1 subunit beta × 1 （Q3ZBH0） T-complex protein 1 subunit × 1 T-complex protein 1 subunit alpha × 1 （Q32L40） T-complex protein 1 subunit eta × 1 （Q2NKZ1）	ELECTRON MICROSCOPY cryo-EM vitrification conditions：two-side blotting for 1 second before plunging；101 K；Cryogen ETHANE；vitrification using ethane as cryogen	Resolution 4.00 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.

Other PDB	Difference from Current Entry 3IYG	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
4B2T The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning Deposited 2012-07-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric	Chain D 1–542（542 aa） Chain d 1–542（542 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 5.50 Å R-free 0.399
9KCF Bovine Flagellar TRiC Deposited 2024-11-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric	Chain D 1–542（542 aa） Chain L 1–542（542 aa）	Not recorded	MG MAGNESIUM ION × 6 ADP ADENOSINE-5'-DIPHOSPHATE × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TCPD_BOVIN
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain D； PDBConstruct 1–518； UniProt 25–542

T-complex protein 1 subunit beta

OrganismNot specified

UniProt Q3ZBH0

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 × 8 PDB declaration: octameric（8） Consistent with protein copy count	Chain B； UniProt 14–526	Not recorded	T-complex protein 1 subunit theta × 1 （Q3ZCI9） T-complex protein 1 subunit gamma × 1 （Q3T0K2） T-complex protein 1 subunit zeta × 1 （Q3MHL7） T-complex protein 1 subunit delta × 1 （Q2T9X2） T-complex protein 1 subunit × 1 T-complex protein 1 subunit alpha × 1 （Q32L40） T-complex protein 1 subunit eta × 1 （Q2NKZ1）	ELECTRON MICROSCOPY cryo-EM vitrification conditions：two-side blotting for 1 second before plunging；101 K；Cryogen ETHANE；vitrification using ethane as cryogen	Resolution 4.00 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.

Other PDB	Difference from Current Entry 3IYG	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3KTT Atomic model of bovine TRiC CCT2(beta) subunit derived from a 4.0 Angstrom cryo-EM map Deposited 2009-11-25	Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 14–526（513 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM vitrification conditions Cryogen ETHANE；vitrification using ethane as cryogen	Resolution 4.00 Å
4A0O Symmetry-free cryo-EM map of TRiC in the nucleotide-free (apo) state Deposited 2011-09-10	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 16 PDB declaration: hexadecameric	Chain A 14–526（513 aa） Fragment：RESIDUES 14-526 Chain B 14–526（513 aa） Fragment：RESIDUES 14-526 Chain C 14–526（513 aa） Fragment：RESIDUES 14-526 Chain D 14–526（513 aa） Fragment：RESIDUES 14-526 Chain E 14–526（513 aa） Fragment：RESIDUES 14-526 Chain F 14–526（513 aa） Fragment：RESIDUES 14-526 Chain G 14–526（513 aa） Fragment：RESIDUES 14-526 Chain H 14–526（513 aa） Fragment：RESIDUES 14-526 Chain I 14–526（513 aa） Fragment：RESIDUES 14-526 Chain J 14–526（513 aa） Fragment：RESIDUES 14-526 Chain K 14–526（513 aa） Fragment：RESIDUES 14-526 Chain L 14–526（513 aa） Fragment：RESIDUES 14-526 Chain M 14–526（513 aa） Fragment：RESIDUES 14-526 Chain N 14–526（513 aa） Fragment：RESIDUES 14-526 Chain O 14–526（513 aa） Fragment：RESIDUES 14-526 Chain P 14–526（513 aa） Fragment：RESIDUES 14-526	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM vitrification conditions Cryogen ETHANE；LIQUID ETHEN	Resolution 10.50 Å
4A0V model refined against the Symmetry-free cryo-EM map of TRiC-AMP-PNP Deposited 2011-09-13	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 16 PDB declaration: hexadecameric	Chain A 14–526（513 aa） Chain B 14–526（513 aa） Chain C 14–526（513 aa） Chain D 14–526（513 aa） Chain E 14–526（513 aa） Chain F 14–526（513 aa） Chain G 14–526（513 aa） Chain H 14–526（513 aa） Chain I 14–526（513 aa） Chain J 14–526（513 aa） Chain K 14–526（513 aa） Chain L 14–526（513 aa） Chain M 14–526（513 aa） Chain N 14–526（513 aa） Chain O 14–526（513 aa） Chain P 14–526（513 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM vitrification conditions Cryogen ETHANE	Resolution 10.70 Å
4A0W model built against symmetry-free cryo-EM map of TRiC-ADP-AlFx Deposited 2011-09-13	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 16 PDB declaration: hexadecameric	Chain A 14–526（513 aa） Chain B 14–526（513 aa） Chain C 14–526（513 aa） Chain D 14–526（513 aa） Chain E 14–526（513 aa） Chain F 14–526（513 aa） Chain G 14–526（513 aa） Chain H 14–526（513 aa） Chain I 14–526（513 aa） Chain J 14–526（513 aa） Chain K 14–526（513 aa） Chain L 14–526（513 aa） Chain M 14–526（513 aa） Chain N 14–526（513 aa） Chain O 14–526（513 aa） Chain P 14–526（513 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM vitrification conditions Cryogen ETHANE	Resolution 13.90 Å
4A13 model refined against symmetry-free cryo-EM map of TRiC-ADP Deposited 2011-09-13	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 16 PDB declaration: hexadecameric	Chain A 14–526（513 aa） Chain B 14–526（513 aa） Chain C 14–526（513 aa） Chain D 14–526（513 aa） Chain E 14–526（513 aa） Chain F 14–526（513 aa） Chain G 14–526（513 aa） Chain H 14–526（513 aa） Chain I 14–526（513 aa） Chain J 14–526（513 aa） Chain K 14–526（513 aa） Chain L 14–526（513 aa） Chain M 14–526（513 aa） Chain N 14–526（513 aa） Chain O 14–526（513 aa） Chain P 14–526（513 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM vitrification conditions Cryogen ETHANE	Resolution 11.30 Å
4B2T The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning Deposited 2012-07-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric	Chain B 1–535（535 aa） Chain b 1–535（535 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 5.50 Å R-free 0.399
9FQR 96-nm repeat of axonemal doublet microtubules from bovine sperm Deposited 2024-06-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 1574 PDB declaration: 1574-meric	Chain Im 1–535（535 aa） Chain In 1–535（535 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 342 MG MAGNESIUM ION × 345 GDP GUANOSINE-5'-DIPHOSPHATE × 345	ELECTRON MICROSCOPY cryo-EM buffer pH 7.9 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 5.00 Å
9KCF Bovine Flagellar TRiC Deposited 2024-11-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric	Chain B 1–535（535 aa） Chain J 1–535（535 aa）	Not recorded	MG MAGNESIUM ION × 6 ADP ADENOSINE-5'-DIPHOSPHATE × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TCPB_BOVIN
Isoform	—
PDB entities	5
Chains and sequence ranges	Author chain B； PDBConstruct 1–513； UniProt 14–526

T-complex protein 1 subunit alpha

OrganismNot specified

UniProt Q32L40

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 × 8 PDB declaration: octameric（8） Consistent with protein copy count	Chain A； UniProt 7–535	Not recorded	T-complex protein 1 subunit theta × 1 （Q3ZCI9） T-complex protein 1 subunit gamma × 1 （Q3T0K2） T-complex protein 1 subunit zeta × 1 （Q3MHL7） T-complex protein 1 subunit delta × 1 （Q2T9X2） T-complex protein 1 subunit beta × 1 （Q3ZBH0） T-complex protein 1 subunit × 1 T-complex protein 1 subunit eta × 1 （Q2NKZ1）	ELECTRON MICROSCOPY cryo-EM vitrification conditions：two-side blotting for 1 second before plunging；101 K；Cryogen ETHANE；vitrification using ethane as cryogen	Resolution 4.00 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.

Other PDB	Difference from Current Entry 3IYG	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
4B2T The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning Deposited 2012-07-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric	Chain A 1–556（556 aa） Chain a 1–556（556 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 5.50 Å R-free 0.399
9KCF Bovine Flagellar TRiC Deposited 2024-11-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric	Chain H 1–556（556 aa） Chain I 1–556（556 aa）	Not recorded	MG MAGNESIUM ION × 6 ADP ADENOSINE-5'-DIPHOSPHATE × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TCPA_BOVIN
Isoform	—
PDB entities	7
Chains and sequence ranges	Author chain A； PDBConstruct 1–529； UniProt 7–535

T-complex protein 1 subunit eta

OrganismNot specified

UniProt Q2NKZ1

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 × 8 PDB declaration: octameric（8） Consistent with protein copy count	Chain H； UniProt 10–524	Not recorded	T-complex protein 1 subunit theta × 1 （Q3ZCI9） T-complex protein 1 subunit gamma × 1 （Q3T0K2） T-complex protein 1 subunit zeta × 1 （Q3MHL7） T-complex protein 1 subunit delta × 1 （Q2T9X2） T-complex protein 1 subunit beta × 1 （Q3ZBH0） T-complex protein 1 subunit × 1 T-complex protein 1 subunit alpha × 1 （Q32L40）	ELECTRON MICROSCOPY cryo-EM vitrification conditions：two-side blotting for 1 second before plunging；101 K；Cryogen ETHANE；vitrification using ethane as cryogen	Resolution 4.00 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.

Other PDB	Difference from Current Entry 3IYG	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
4B2T The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning Deposited 2012-07-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric	Chain H 1–543（543 aa） Chain h 1–543（543 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 5.50 Å R-free 0.399
9FQR 96-nm repeat of axonemal doublet microtubules from bovine sperm Deposited 2024-06-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 1574 PDB declaration: 1574-meric	Chain Gv 1–543（543 aa） Chain Gw 1–543（543 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 342 MG MAGNESIUM ION × 345 GDP GUANOSINE-5'-DIPHOSPHATE × 345	ELECTRON MICROSCOPY cryo-EM buffer pH 7.9 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 5.00 Å
9KCF Bovine Flagellar TRiC Deposited 2024-11-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric	Chain F 1–543（543 aa） Chain N 1–543（543 aa）	Not recorded	MG MAGNESIUM ION × 6 ADP ADENOSINE-5'-DIPHOSPHATE × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TCPH_BOVIN
Isoform	—
PDB entities	8
Chains and sequence ranges	Author chain H； PDBConstruct 1–515； UniProt 10–524

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3iyg
Deposition date deposition_date	2009-11-28
Structure title title	Ca model of bovine TRiC/CCT derived from a 4.0 Angstrom cryo-EM map
Keywords keywords	;TRiC/CCT, Asymmetric, Cryo-EM, subunit arrangement, ATP-binding, Chaperone, Isopeptide bond, Nucleotide-binding, Phosphoprotein, Disulfide bond ;; CHAPERONE
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	57.04 Å
Radius of gyration Rg (electron density) rg_electron	56.43 Å
Forward intensity I(0) i0	2871500000.00
Molecular weight molecular_weight	451370.0 kDa
Excluded volume excluded_volume	556740 Å³
Envelope volume envelope_volume	664540 Å³
Hydration-shell volume shell_volume	102750 Å³
Envelope diameter envelope_diameter	166.5 Å
Shell Rg shell_rg	60.70 Å
Envelope Rg envelope_rg	49.51 Å
Shape Rg shape_rg	56.54 Å
Total Rg total_rg	56.52 Å
Total atoms total_atoms	—
Residues n_residues	—
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	165.3 Å
Rg (real space) rg_real	56.64 Å
Rg uncertainty (real space) rg_real_error	0.84 Å
I(0) (real space) i0_real	2.8710e+09
I(0) uncertainty (real space) i0_real_error	5.0700e+07
Rg (reciprocal space) rg_reciprocal	57.35 Å
I(0) (reciprocal space) i0_reciprocal	2874000000.0000
Solution quality estimate total_estimate	0.8564
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	82.7 Å
Skewness Skewness skewness	-0.102
Kurtosis Kurtosis kurtosis	-0.726
Angular range angular_range	— – 0.1400 Å⁻¹
Current regularization parameter α current_alpha	0.0003
Highest regularization parameter α highest_alpha	125100000.0000
Real-space data points n_real_points	29
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.964; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.268

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (8)

Entity 1 Entity 1 polymer

Description description	T-complex protein 1 subunit theta
Molecular weight formula_weight	55833.9 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	Q
Atom count atom_count	4134

EGAKHFSGLEEAVYRNIQACKELAQTTRTAYGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKMIVMASHMQEQEVGDGTNFVLVFAGALLELAEELLRLGLSVSEVIEGYEIACKKAHEILPDLVCCSAKNLRDVDEVSSLLHTSVMSKQYGNEVFLAKLIAQACVSIFPDSGHFNVDNIRVCKILGSGVHSSSVLHGMVFKKETEGDVTSVKDAKIAVYSCPFDGMITETKGTVLIKSAEELMNFSKGEENLMDAQVKAIADTGANVVVTGGRVADMALHYANKYNIMLVRLNSKWDLRRLCKTVGATALPRLNPPVLEEMGHCDSVYLSEVGDTQVVVFKHEKEDGAISTIVLRGSTDNLMDDIERAVDDGVNTFKVLTRDKRLVPGGGATEIELAKQITSYGETCPGLEQYAIKKFAEAFEAIPRALAENSGVKANEVISKLYAVHQEGNKNVGLDIEAEVPAVKDMLEAGVLDTYLGKYWAIKLATNAAVTVLRVDQIIMAK

Entity 2 Entity 2 polymer

Description description	T-complex protein 1 subunit gamma
Molecular weight formula_weight	57486.3 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G

NTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDTSNRDTMLNIINSSITTKVISRWSSLACNIALDAVKTVQFEENGRKEIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKKGESQTDIEITREEDFTRILQMEEEYIQQLCEDIIQLKPDVVITEKGISDLAQHYLMRANITAIRRVRKTDNNRIARACGARIVSRPEELREEDVGTGAGLLEIKKIGDEYFTFITECKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQENCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHK

Entity 3 Entity 3 polymer

Description description	T-complex protein 1 subunit zeta
Molecular weight formula_weight	56602.3 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	Z

PKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEQVKVSKEMDRETLIDVARTSLRTKVHAELADVLTEAVVDSILAIKKQDEPIDLFMVEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEEREKLVKAERKFIEDRVKKIIELKKKVCGDSDKGFVVINQKGIDPFSLDALAKEGIIALRRAKRRNMERLTLACGGIALNSLDDLNPDCLLGHAGVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAIRDGLRAVKNAIDDGCVVPGAGAVEVAMAEALVKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEHSESGQLVGVDLNTGEPMVAAEAGIWDNYCVKKQLLHSCTVIATNILLVDEIMRAG

Entity 4 Entity 4 polymer

Description description	T-complex protein 1 subunit delta
Molecular weight formula_weight	56057.9 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D

SAYQDRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVELSDRETLLNSAATSLNSKVVSQYSSLLSPMSVDAVMKVIDPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGITRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYVQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSILRDALSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKPVAHVDQFTADMLGSAELAEEVSLNGSGKLIKITGCASPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELALRLTEYSRTLSGMESYCIRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNILEELVVQPLLVSVSALTLATETVRSILKIDDVVNTR

Entity 5 Entity 5 polymer

Description description	T-complex protein 1 subunit beta
Molecular weight formula_weight	55107.2 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

AGADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAARQALLNSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHVIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFVGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLASRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGKTTAGLDMKEGTIGDMSVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPR

Entity 6 Entity 6 polymer

Description description	T-complex protein 1 subunit
Molecular weight formula_weight	56751.7 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E

DRKSRLMGLEALKSHIMAAKAVANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKISDSVLVDMKNTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVADMQRRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKQVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDFKALQKYEKEKFEEMIRQIKETGANLAVCQWGFDDEANHLLLQNDLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGFAGLVKEISFGTTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALAENSGMNPIQTMTEVRARQVKEVNPALGIDCLHKGTNDMKHQHVIETLIGKKQQISLATQMVRMILKIDDIRKPG

Entity 7 Entity 7 polymer

Description description	T-complex protein 1 subunit alpha
Molecular weight formula_weight	57495.4 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A

VFGDRSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYISENLIINTDELGRDCLINAAKTSMSSKVIGINGDFFANLVVDAVLAIKYTDIRGQPRYPVNSINVLKAHGRSQMESMLINGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGATVLSTLANLEGEETFEASMLGQAEEVVQERICDDELILIKNTKARTSASVILRGANDFMCDEMERSLHDALCVVKRVLESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNPERKNLKWIGLDLVNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHP

Entity 8 Entity 8 polymer

Description description	T-complex protein 1 subunit eta
Molecular weight formula_weight	56614.2 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H

KEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKEDKVEQRKLLEKCAMTALSSKLISQQKAFFAKMVVDAVMMLDDLLQLKMIGIKKVQGGALEESQLVAGVAFKKTFSYAGFEMQPKKYHNPMIALLNVELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGSIQTSVNALSSDVLGRCQVFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGMWYGVDINTEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETIKNPR

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

Resolution resolution	4.00 Å
Resolution测定方法 resolution_method	Projection matching
颗粒数 num_particles	101000

fit	/app/data/saxs_computation/iy/3iyg/3iyg.fit
pddf	/app/data/pr_computation/iy/3iyg/3iyg.pr.out
profile	/app/data/saxs_computation/iy/3iyg/3iyg.dat

Ca model of bovine TRiC/CCT derived from a 4.0 Angstrom cryo-EM map

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

T-complex protein 1 subunit theta

State in the Current Structure

Other States of the Same Protein in the Database

T-complex protein 1 subunit gamma

State in the Current Structure

Other States of the Same Protein in the Database

T-complex protein 1 subunit zeta

State in the Current Structure

Other States of the Same Protein in the Database

T-complex protein 1 subunit delta

State in the Current Structure

Other States of the Same Protein in the Database

T-complex protein 1 subunit beta

State in the Current Structure

Other States of the Same Protein in the Database

T-complex protein 1 subunit alpha

State in the Current Structure

Other States of the Same Protein in the Database

T-complex protein 1 subunit eta

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (8)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

Entity 5 Entity 5 polymer

Polymer Polymer

Entity 6 Entity 6 polymer

Polymer Polymer

Entity 7 Entity 7 polymer

Polymer Polymer

Entity 8 Entity 8 polymer

Polymer Polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)