9g3y

Structure of the Native CMG-decorated gamma-Tubulin Ring Complex from Pig Brain

Method: ELECTRON MICROSCOPY D_max: 377.0 Å Quality: GOOD

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

Gamma-tubulin complex component

Sus scrofa

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 × 45 PDB declaration: 45-meric（45） Consistent with protein copy count	Chain A； UniProt 1–905 Chain C； UniProt 1–905 Chain E； UniProt 1–905 Chain G； UniProt 1–905 Chain M； UniProt 1–905	Not recorded	Gamma-tubulin complex component 3 × 5 （F1RN46） Gamma-tubulin complex component × 2 （A0A8D1V2H0） Gamma-tubulin complex component × 1 （I3L738） Tubulin gamma complex associated protein 6 × 1 （A0A8W4FDV6） Mitotic spindle organizing protein 1 × 3 （A0A4X1VBW8） Mitotic-spindle organizing protein 2A isoform X4 × 4 （F1RK97） Tubulin gamma chain × 14 （A0A287BRH5） CDK5 regulatory subunit-associated protein 2 × 10 （A0A0A0MRG9）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE-PROPANE	Resolution 6.80 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 9G3Y	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9G3X Structure of the Partially-assembled gamma-Tubulin Ring Complex from Pig Brain Deposited 2024-07-12	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain G 1–905（905 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 4.50 Å
9G3Z Structure of the Open gamma-Tubulin Ring Complex from Pig Brain Deposited 2024-07-12	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 34 PDB declaration: 34-meric	Chain A 1–905（905 aa） Chain C 1–905（905 aa） Chain E 1–905（905 aa） Chain G 1–905（905 aa） Chain M 1–905（905 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 4.30 Å

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

View Construct and Data Evidence

UniProt name	A0A8D1IGH3_PIG
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–905； UniProt 1–905 Author chain C； PDBConstruct 1–905； UniProt 1–905 Author chain E； PDBConstruct 1–905； UniProt 1–905 Author chain G； PDBConstruct 1–905； UniProt 1–905 Author chain M； PDBConstruct 1–905； UniProt 1–905

Gamma-tubulin complex component 3

Sus scrofa

UniProt F1RN46

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 × 45 PDB declaration: 45-meric（45） Consistent with protein copy count	Chain B； UniProt 1–910 Chain D； UniProt 1–910 Chain F； UniProt 1–910 Chain H； UniProt 1–910 Chain N； UniProt 1–910	Not recorded	Gamma-tubulin complex component × 5 （A0A8D1IGH3） Gamma-tubulin complex component × 2 （A0A8D1V2H0） Gamma-tubulin complex component × 1 （I3L738） Tubulin gamma complex associated protein 6 × 1 （A0A8W4FDV6） Mitotic spindle organizing protein 1 × 3 （A0A4X1VBW8） Mitotic-spindle organizing protein 2A isoform X4 × 4 （F1RK97） Tubulin gamma chain × 14 （A0A287BRH5） CDK5 regulatory subunit-associated protein 2 × 10 （A0A0A0MRG9）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE-PROPANE	Resolution 6.80 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 9G3Y	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9G3X Structure of the Partially-assembled gamma-Tubulin Ring Complex from Pig Brain Deposited 2024-07-12	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain H 1–910（910 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 4.50 Å
9G3Z Structure of the Open gamma-Tubulin Ring Complex from Pig Brain Deposited 2024-07-12	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 34 PDB declaration: 34-meric	Chain B 1–910（910 aa） Chain D 1–910（910 aa） Chain F 1–910（910 aa） Chain H 1–910（910 aa） Chain N 1–910（910 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 4.30 Å
9G40 Structure of the Position 7 CMG-decorated gamma-Tubulin Ring Complex from Pig Brain Deposited 2024-07-12	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain F 1–910（910 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；Listed in "g-TuRC cryo-EM sample preparation" section. cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 4.30 Å

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

View Construct and Data Evidence

UniProt name	F1RN46_PIG
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–910； UniProt 1–910 Author chain D； PDBConstruct 1–910； UniProt 1–910 Author chain F； PDBConstruct 1–910； UniProt 1–910 Author chain H； PDBConstruct 1–910； UniProt 1–910 Author chain N； PDBConstruct 1–910； UniProt 1–910

Gamma-tubulin complex component

Sus scrofa

UniProt A0A8D1V2H0

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 × 45 PDB declaration: 45-meric（45） Consistent with protein copy count	Chain I； UniProt 1–667 Chain K； UniProt 1–667	Not recorded	Gamma-tubulin complex component × 5 （A0A8D1IGH3） Gamma-tubulin complex component 3 × 5 （F1RN46） Gamma-tubulin complex component × 1 （I3L738） Tubulin gamma complex associated protein 6 × 1 （A0A8W4FDV6） Mitotic spindle organizing protein 1 × 3 （A0A4X1VBW8） Mitotic-spindle organizing protein 2A isoform X4 × 4 （F1RK97） Tubulin gamma chain × 14 （A0A287BRH5） CDK5 regulatory subunit-associated protein 2 × 10 （A0A0A0MRG9）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE-PROPANE	Resolution 6.80 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 9G3Y	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9G3X Structure of the Partially-assembled gamma-Tubulin Ring Complex from Pig Brain Deposited 2024-07-12	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain I 1–667（667 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 4.50 Å
9G3Z Structure of the Open gamma-Tubulin Ring Complex from Pig Brain Deposited 2024-07-12	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 34 PDB declaration: 34-meric	Chain I 1–667（667 aa） Chain K 1–667（667 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 4.30 Å

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

View Construct and Data Evidence

UniProt name	A0A8D1V2H0_PIG
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain I； PDBConstruct 1–667； UniProt 1–667 Author chain K； PDBConstruct 1–667； UniProt 1–667

Gamma-tubulin complex component

Sus scrofa

UniProt I3L738

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 × 45 PDB declaration: 45-meric（45） Consistent with protein copy count	Chain J； UniProt 1–1061	Not recorded	Gamma-tubulin complex component × 5 （A0A8D1IGH3） Gamma-tubulin complex component 3 × 5 （F1RN46） Gamma-tubulin complex component × 2 （A0A8D1V2H0） Tubulin gamma complex associated protein 6 × 1 （A0A8W4FDV6） Mitotic spindle organizing protein 1 × 3 （A0A4X1VBW8） Mitotic-spindle organizing protein 2A isoform X4 × 4 （F1RK97） Tubulin gamma chain × 14 （A0A287BRH5） CDK5 regulatory subunit-associated protein 2 × 10 （A0A0A0MRG9）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE-PROPANE	Resolution 6.80 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 9G3Y	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9G3X Structure of the Partially-assembled gamma-Tubulin Ring Complex from Pig Brain Deposited 2024-07-12	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain J 1–1061（1061 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 4.50 Å

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	I3L738_PIG
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain J； PDBConstruct 1–1061； UniProt 1–1061

Tubulin gamma complex associated protein 6

Sus scrofa

UniProt A0A8W4FDV6

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 × 45 PDB declaration: 45-meric（45） Consistent with protein copy count	Chain L； UniProt 1–1715	Not recorded	Gamma-tubulin complex component × 5 （A0A8D1IGH3） Gamma-tubulin complex component 3 × 5 （F1RN46） Gamma-tubulin complex component × 2 （A0A8D1V2H0） Gamma-tubulin complex component × 1 （I3L738） Mitotic spindle organizing protein 1 × 3 （A0A4X1VBW8） Mitotic-spindle organizing protein 2A isoform X4 × 4 （F1RK97） Tubulin gamma chain × 14 （A0A287BRH5） CDK5 regulatory subunit-associated protein 2 × 10 （A0A0A0MRG9）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE-PROPANE	Resolution 6.80 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 9G3Y	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9G3Z Structure of the Open gamma-Tubulin Ring Complex from Pig Brain Deposited 2024-07-12	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 34 PDB declaration: 34-meric	Chain L 1–1715（1715 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 4.30 Å

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A8W4FDV6_PIG
Isoform	—
PDB entities	5
Chains and sequence ranges	Author chain L； PDBConstruct 1–1715； UniProt 1–1715

Mitotic spindle organizing protein 1

Sus scrofa

UniProt A0A4X1VBW8

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 × 45 PDB declaration: 45-meric（45） Consistent with protein copy count	Chain O； UniProt 1–79 Chain P； UniProt 1–79 Chain Q； UniProt 1–79	Not recorded	Gamma-tubulin complex component × 5 （A0A8D1IGH3） Gamma-tubulin complex component 3 × 5 （F1RN46） Gamma-tubulin complex component × 2 （A0A8D1V2H0） Gamma-tubulin complex component × 1 （I3L738） Tubulin gamma complex associated protein 6 × 1 （A0A8W4FDV6） Mitotic-spindle organizing protein 2A isoform X4 × 4 （F1RK97） Tubulin gamma chain × 14 （A0A287BRH5） CDK5 regulatory subunit-associated protein 2 × 10 （A0A0A0MRG9）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE-PROPANE	Resolution 6.80 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 9G3Y	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9G3X Structure of the Partially-assembled gamma-Tubulin Ring Complex from Pig Brain Deposited 2024-07-12	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain P 1–79（79 aa） Chain R 1–79（79 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 4.50 Å
9G3Z Structure of the Open gamma-Tubulin Ring Complex from Pig Brain Deposited 2024-07-12	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 34 PDB declaration: 34-meric	Chain O 1–79（79 aa） Chain P 1–79（79 aa） Chain Q 1–79（79 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 4.30 Å

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

View Construct and Data Evidence

UniProt name	A0A4X1VBW8_PIG
Isoform	—
PDB entities	6
Chains and sequence ranges	Author chain O； PDBConstruct 1–79； UniProt 1–79 Author chain P； PDBConstruct 1–79； UniProt 1–79 Author chain Q； PDBConstruct 1–79； UniProt 1–79

Mitotic-spindle organizing protein 2A isoform X4

Sus scrofa

UniProt F1RK97

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 × 45 PDB declaration: 45-meric（45） Consistent with protein copy count	Chain V； UniProt 1–155 Chain W； UniProt 1–155 Chain X； UniProt 1–155 Chain Y； UniProt 1–155	Not recorded	Gamma-tubulin complex component × 5 （A0A8D1IGH3） Gamma-tubulin complex component 3 × 5 （F1RN46） Gamma-tubulin complex component × 2 （A0A8D1V2H0） Gamma-tubulin complex component × 1 （I3L738） Tubulin gamma complex associated protein 6 × 1 （A0A8W4FDV6） Mitotic spindle organizing protein 1 × 3 （A0A4X1VBW8） Tubulin gamma chain × 14 （A0A287BRH5） CDK5 regulatory subunit-associated protein 2 × 10 （A0A0A0MRG9）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE-PROPANE	Resolution 6.80 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 9G3Y	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9G3Z Structure of the Open gamma-Tubulin Ring Complex from Pig Brain Deposited 2024-07-12	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 34 PDB declaration: 34-meric	Chain Y 1–155（155 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 4.30 Å
9G40 Structure of the Position 7 CMG-decorated gamma-Tubulin Ring Complex from Pig Brain Deposited 2024-07-12	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain X 1–155（155 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；Listed in "g-TuRC cryo-EM sample preparation" section. cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 4.30 Å

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

View Construct and Data Evidence

UniProt name	F1RK97_PIG
Isoform	—
PDB entities	7
Chains and sequence ranges	Author chain V； PDBConstruct 1–155； UniProt 1–155 Author chain W； PDBConstruct 1–155； UniProt 1–155 Author chain X； PDBConstruct 1–155； UniProt 1–155 Author chain Y； PDBConstruct 1–155； UniProt 1–155

Tubulin gamma chain

Sus scrofa

UniProt A0A287BRH5

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 × 45 PDB declaration: 45-meric（45） Consistent with protein copy count	Chain a； UniProt 1–451 Chain b； UniProt 1–451 Chain c； UniProt 1–451 Chain d； UniProt 1–451 Chain e； UniProt 1–451 Chain f； UniProt 1–451 Chain g； UniProt 1–451 Chain h； UniProt 1–451 Chain i； UniProt 1–451 Chain j； UniProt 1–451 Chain k； UniProt 1–451 Chain l； UniProt 1–451 Chain m； UniProt 1–451 Chain n； UniProt 1–451	Not recorded	Gamma-tubulin complex component × 5 （A0A8D1IGH3） Gamma-tubulin complex component 3 × 5 （F1RN46） Gamma-tubulin complex component × 2 （A0A8D1V2H0） Gamma-tubulin complex component × 1 （I3L738） Tubulin gamma complex associated protein 6 × 1 （A0A8W4FDV6） Mitotic spindle organizing protein 1 × 3 （A0A4X1VBW8） Mitotic-spindle organizing protein 2A isoform X4 × 4 （F1RK97） CDK5 regulatory subunit-associated protein 2 × 10 （A0A0A0MRG9）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE-PROPANE	Resolution 6.80 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 9G3Y	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9G3X Structure of the Partially-assembled gamma-Tubulin Ring Complex from Pig Brain Deposited 2024-07-12	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain g 1–451（451 aa） Chain h 1–451（451 aa） Chain i 1–451（451 aa） Chain j 1–451（451 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 4.50 Å
9G3Z Structure of the Open gamma-Tubulin Ring Complex from Pig Brain Deposited 2024-07-12	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 34 PDB declaration: 34-meric	Chain a 1–451（451 aa） Chain b 1–451（451 aa） Chain c 1–451（451 aa） Chain d 1–451（451 aa） Chain e 1–451（451 aa） Chain f 1–451（451 aa） Chain g 1–451（451 aa） Chain h 1–451（451 aa） Chain i 1–451（451 aa） Chain j 1–451（451 aa） Chain k 1–451（451 aa） Chain l 1–451（451 aa） Chain m 1–451（451 aa） Chain n 1–451（451 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 4.30 Å

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

View Construct and Data Evidence

UniProt name	A0A287BRH5_PIG
Isoform	—
PDB entities	8
Chains and sequence ranges	Author chain a； PDBConstruct 1–451； UniProt 1–451 Author chain b； PDBConstruct 1–451； UniProt 1–451 Author chain c； PDBConstruct 1–451； UniProt 1–451 Author chain d； PDBConstruct 1–451； UniProt 1–451 Author chain e； PDBConstruct 1–451； UniProt 1–451 Author chain f； PDBConstruct 1–451； UniProt 1–451 Author chain g； PDBConstruct 1–451； UniProt 1–451 Author chain h； PDBConstruct 1–451； UniProt 1–451 Author chain i； PDBConstruct 1–451； UniProt 1–451 Author chain j； PDBConstruct 1–451； UniProt 1–451 Author chain k； PDBConstruct 1–451； UniProt 1–451 Author chain l； PDBConstruct 1–451； UniProt 1–451 Author chain m； PDBConstruct 1–451； UniProt 1–451 Author chain n； PDBConstruct 1–451； UniProt 1–451

CDK5 regulatory subunit-associated protein 2

Homo sapiens

UniProt A0A0A0MRG9

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 × 45 PDB declaration: 45-meric（45） Consistent with protein copy count	Chain o； UniProt 1–1663 Chain p； UniProt 1–1663 Chain q； UniProt 1–1663 Chain r； UniProt 1–1663 Chain s； UniProt 1–1663 Chain t； UniProt 1–1663 Chain u； UniProt 1–1663 Chain v； UniProt 1–1663 Chain w； UniProt 1–1663 Chain x； UniProt 1–1663	Not recorded	Gamma-tubulin complex component × 5 （A0A8D1IGH3） Gamma-tubulin complex component 3 × 5 （F1RN46） Gamma-tubulin complex component × 2 （A0A8D1V2H0） Gamma-tubulin complex component × 1 （I3L738） Tubulin gamma complex associated protein 6 × 1 （A0A8W4FDV6） Mitotic spindle organizing protein 1 × 3 （A0A4X1VBW8） Mitotic-spindle organizing protein 2A isoform X4 × 4 （F1RK97） Tubulin gamma chain × 14 （A0A287BRH5）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE-PROPANE	Resolution 6.80 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 9G3Y	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9G3Z Structure of the Open gamma-Tubulin Ring Complex from Pig Brain Deposited 2024-07-12	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 34 PDB declaration: 34-meric	Chain w 1–1663（1663 aa） Chain x 1–1663（1663 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 4.30 Å
9QVM Cryo-EM reconstruction of the NEDD1 anchor protein and CDK5RAP2 bound to the gamma-tubulin ring complex Deposited 2025-04-11	Different construct Different mutation/modification Different oligomeric state	Assembly 1 Protein heterocomplex Heteromer；Protein × 48 PDB declaration: 48-meric	Chain w 1–1663（1663 aa） Chain x 1–1663（1663 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 6.80 Å

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

View Construct and Data Evidence

UniProt name	A0A0A0MRG9_HUMAN
Isoform	—
PDB entities	9
Chains and sequence ranges	Author chain o； PDBConstruct 1–1663； UniProt 1–1663 Author chain p； PDBConstruct 1–1663； UniProt 1–1663 Author chain q； PDBConstruct 1–1663； UniProt 1–1663 Author chain r； PDBConstruct 1–1663； UniProt 1–1663 Author chain s； PDBConstruct 1–1663； UniProt 1–1663 Author chain t； PDBConstruct 1–1663； UniProt 1–1663 Author chain u； PDBConstruct 1–1663； UniProt 1–1663 Author chain v； PDBConstruct 1–1663； UniProt 1–1663 Author chain w； PDBConstruct 1–1663； UniProt 1–1663 Author chain x； PDBConstruct 1–1663； UniProt 1–1663

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	9g3y
Deposition date deposition_date	2024-07-12
Structure title title	Structure of the Native CMG-decorated gamma-Tubulin Ring Complex from Pig Brain
Keywords keywords	Tubulin Complex, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
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	— Å
Radius of gyration Rg (electron density) rg_electron	112.50 Å
Forward intensity I(0) i0	27121000000.00
Molecular weight molecular_weight	1153300.0 kDa
Excluded volume excluded_volume	1329300 Å³
Envelope volume envelope_volume	4059200 Å³
Hydration-shell volume shell_volume	307770 Å³
Envelope diameter envelope_diameter	321.5 Å
Shell Rg shell_rg	113.50 Å
Envelope Rg envelope_rg	100.10 Å
Shape Rg shape_rg	112.50 Å
Total Rg total_rg	112.50 Å
Total atoms total_atoms	118940
Residues n_residues	16637
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	377.0 Å
Rg (real space) rg_real	116.30 Å
Rg uncertainty (real space) rg_real_error	2.62 Å
I(0) (real space) i0_real	2.7120e+10
I(0) uncertainty (real space) i0_real_error	7.2460e+08
Rg (reciprocal space) rg_reciprocal	115.50 Å
I(0) (reciprocal space) i0_reciprocal	27310000000.0000
Solution quality estimate total_estimate	0.8663
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	134.6 Å
Skewness Skewness skewness	0.151
Kurtosis Kurtosis kurtosis	-0.384
Angular range angular_range	— – 0.0700 Å⁻¹
Current regularization parameter α current_alpha	0.9796
Highest regularization parameter α highest_alpha	883500000.0000
Real-space data points n_real_points	15
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.880; Stabil: 0.902; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.001

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (9)

Entity 1 Entity 1 polymer

Description description	Gamma-tubulin complex component
Molecular weight formula_weight	102609.7 kDa
Source method src_method	man
Copy count entity_count	5

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C,E,G,M
Atom count atom_count	118940

MSEFRIHHDVNELLSLLRVHGGDGAEVYIDLLQKNRTPYVTTTVSAHSAKVKIAEFSRTPEDFLKKYDELKSKNTRNLDPLVYLLSKLMEDRETLQYLQQNAKERAELAASAAASSTASFGASATASKISMQELEELRKQLGSVATGPTWQQSLELTRKMLRDKQSKKNSGQRLPVLPAWVYERPALLGDFLPGTGGSADTAVPIGSLPLASQEAAVVEDLLYVLVGVDGRYISAQPLTGRQGRTFLVDPNLDLSIRELVSRILPVAASYSTVTRFIEEKSSFEYGQVNHALAAAMRTLVKEYLVLVTQLEQLQRQGLLSLQKLWFYIQPAMRSLDILASLATSVDKGECIGGATLSLLHDRSFSYTGDSQAQELCLHLTKAASTPYFEILEKWIYRGIIDDPYSEFMVEEHELRKEKIQEDYNDKYWDQRYTVVQRQIPSFLQKMAGKVLSTGKYLNVVRECGHDVTCPVAKEVVYTLKERAYVEQIEKAFSYASKVLLDFLMGEKELLAHLRSIKRYFLMDQGDFFVHFMDLTEEELKKPVDDITPTRLEALLELALRMSTANTDPFKDDLKIDLMPHDLITQLLRVLAIETQQEKAMVHADPTELTLSGLEAFSFDYVVTWPLSLIINRKALTRYQMLFRHMFYCKHVERQLCSVWISNKAAKRFSLHSAKWFAGAFTLRQRMLNFVQNIQSYMMFEVMEPTWHVLEQNLRSASNIDDVLGHHASFLDNCLKDCMLTNPELLRVFSKLMSVCVMFTNCLQRFTQSMKLDSELGHPALEPGAMLGPPTEAERAEERARKELARKCLAEHVDAPQLASSFEATITKFDKNFSAHLLDLLARLSIYSTSDCEHGMASVISRLDFNGFYTERLERLSAERSQKAAPPVPGPRGPPALVPRVAVTAQ

来源 Source

来源生物 organism	Sus scrofa
通用名 common_name	pig
NCBI Class编号 ncbi_taxonomy_id	9823
宿主生物 host_organism	Sus scrofa

Entity 2 Entity 2 polymer

Description description	Gamma-tubulin complex component 3
Molecular weight formula_weight	103172.5 kDa
Source method src_method	man
Copy count entity_count	5

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D,F,H,N

MATPDQKSPNVLLQNLCCRILGKSEADVAQQFQYAVRVIGSNFAPTVERDEFLVAEKIKKELTRQRREADAALFSELHRKLHSQGVLKNKWSILYLLLSLSEDPRKQPSKVSGYAALFAQALPRDAHSTPYYYARPQSLPLNYQERGAPSAQSAGSAGSSGVSSLGTYALNGPTPPPPPPALLPGQPLPAPGVGDGLRQQLGSRLAWTLTASQPSLPSTTSKAVPSSGSRGAARPRREGDAAAGAVEVTEAALVRDILYVFQGIDGKHVKMSNADNCYTVEGKANLSKSLRDTAVRLAELGWLHNKIRKYTDQRSLDRSFGLVGQSFCAALHQELREYYRLLSVLHSQLQLEDDQGVNLGLESSLTLRRLLVWTYDPKMRLKTLAALVDHCQGRKGGELASAVHAYTKTGDPYARSLVQHILSLVSHPVLSFLYRWIYDGELEDTYHEFFVASDPAVKADRLWHDKYALRKPMIPSFMTMDQCRKVLLIGKSINFLHQVCHDQTPTTKMIAVTKSAESPQDAADLFTDLENAFQGKIDAAYFETSKYLLDVLNKKYSLLDHMQAMRRYLLLGQGDFIRHLMDLLKPELVRPATTLYQHNLTGILETAVRATNAQFDSPEILKRLDVRLLEVSPGDTGWDVFSLDYHVDGPIATVFTRECMSHYLRAFNFLWRAKRVEYILTDIRKGHMCNARLLRSMPEFSGVLHHCHILASEMVHFIHQMQYYVTFEVLECSWDELWNRVQRAQDLDHIIAAHEAFLGTVISRCLLDSDSRALLNQLRAVFDQIIELQNTQDAIYRAALEELQRRLQFEEKKKQREAEGQWGVSAAEEEQEKRRVQEFQESIPKMCSQLRILTHFYQGVVQQFLVSLTTSSDESLRFLSFRLDFNEHYRAREPRLRVSLGTRGRRSSHT

来源 Source

来源生物 organism	Sus scrofa
通用名 common_name	pig
NCBI Class编号 ncbi_taxonomy_id	9823
宿主生物 host_organism	Sus scrofa

Entity 3 Entity 3 polymer

Description description	Gamma-tubulin complex component
Molecular weight formula_weight	76104.9 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	I,K

MIHELLLALSGYPGSIFTWNKRGGLQVSQDFPFLHPSETSVLNRLCRLGTDYIRFTEFIEQYTGHVQQQDHHPSQQGQGGLHGIYLRAFCTGLDSVLQPYRQALLDLEQEFLADPHLSISHINYSLDQFQLLFPSVMVVVEQIKSQKIHGCQILETVYKHSCGGLPPVRSALEKILAVCHGVMYKQLSAWMLHGLLLDQHEEFFIKQGPSSGNVSAQPEEDEEDLGIGGLTGKQLRELQDLRLIEEENMLAPSLKQFSLRVEILPSYIPVRVAEKILFVGESVQMFENQNVNLTRKGSILKDQEDTFAAELHRLKQQPLFSLVDFEQVVDRIRSTVAEHLWKLMVEESDLLGQLKIIKDFYLLGRGELFQAFIDTAQHMLKTPPTAVTEHDVNVAFQQSAHKVLLDDDNLLPLLHLTIEYHGKEHKADATQAREGPSRETSPREAPASGWAALGLSYKVQWPLHILFTPAVLEKYNVVFKYLLSVRRVQAELQHCWALQMQRKHLKSNQTDAVKWRLRNHMAFLVDNLQYYLQVDVLESQFSQLLHQINSTRDFESIRLAHDHFLSNLLAQSFILLKPVFHCLNEILDLCHSFCSLVSQNLGPLDERGAAQLSILVKGFSRQSSLLFKILSSVRNHQINSDLAQLLLRLDYNKYYTQAGGTLGSFGM

来源 Source

来源生物 organism	Sus scrofa
通用名 common_name	pig
NCBI Class编号 ncbi_taxonomy_id	9823
宿主生物 host_organism	Sus scrofa

Entity 4 Entity 4 polymer

Description description	Gamma-tubulin complex component
Molecular weight formula_weight	122040.3 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	J

MASPAPSWTRLDPQQERDVRELIRLVSGVQDEADPNFQLALHFAWSNFRFHRFLDVNSHKVEKTIEGIYEKFIIHSDLSKAASWKRLTDEFLNASLPSIKEIKTDAHYSILSLLLCLSDSPSNSNYVETPRNKEVEKKDDFDWGKYLMEGEEIDLGPNVDTPNWSEESEDEDDPQPLSREDSGIQVDRTPLEEQDQSRKPASRVSWKVDEPDARSWLEQHVVRQYWTTRSSKFPHSLHLHSNLAAVWDQHLYSSDPLYVPDDRVSVTETQVIRETLWLLSGVKKLFIFQLIDGKVAVRNNIMVTHLTHSCLRSVLEQIAAYGQVVFRLQEFIDEVMGHSSESTLPGNGSVPKKSTDAPFRTYQAFMWALYKYFISFKEELSEIEKCIINNDTTVTLAIVVDKLSPRLAQLKVLHKVFSTGVAEVPPDTRNVVRASHLLNTLYKAILEYDNVGEASEQTVSLLFSLWVETVRPYLQIVDEWIVHGHLCDGAREFIIQRNKNVPVNHRDFWYATYTLYSVSEKTENEEKMSDNASASSGSDQGPSSRQHTMVSFLKPVLKQIIMAGKSMQLLKNLQCAESTTCQAMARDAERKSLYTLFLESVQSRLRHGEDATAQALTEQQATRETLIKMQSIAERHLELDDVHDPLLAINFARLYLEQSDFHEKFAGGDICVDRSSESVTCQTFELTLRSCLYPHIDKQYLDCCGNLMRTLKKDYRLVEYLQAMRNFFLMEGGDTMYDFYTSIFDKIREKETWQNVSFLNVQLQEAVGQRYPEDSSRLSISFENTDTAKKKLPVHTLDGLTLSYKVPWPVDIVISLECQKIYNQVFLLLLQIKWAKYSLDVLLFGELASSAEKPQSKEGLLSGQDTAAQFGPQKEPVRQQIHRMFLLRVKLMHFVNSLHNYIMTRILHSTGLEFQHQVEEAKDLDQLIKIHYRYLSTIHDRCLLREKVSFVKEAIMKVLNLALMFADGWQAGLGAWQMESIEKMESDFKNCHMFLVTILNKAVCRGSFPHLESLALSLMAGMEQKREDDLFNHTWGQGDLPNYTCAVRLLGVRKGGGTRPK

来源 Source

来源生物 organism	Sus scrofa
通用名 common_name	pig
NCBI Class编号 ncbi_taxonomy_id	9823
宿主生物 host_organism	Sus scrofa

Entity 5 Entity 5 polymer

Description description	Tubulin gamma complex associated protein 6
Molecular weight formula_weight	188644.8 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	L

MASVPQLLDDLCEALLPAAKAHLGQRRGSRKRAKQSLKKVAYNALFTNLFQDEARKLQPDLPRLPVKNRILMLSFDLRVGGLAAEADRLEELVEGLETAPRGPLAELGSVLDLLVQLAGSGPPRVLQRRRDYFLPKEHVGRNVRYGGYDCCHLSGIEADVRSIISGEEELCRDLIRKTLQVMEAAPGTGLPAFGLSSYGDPYGDRFERDTRVSLFGALVHSRTADLDVRLDLPPVPDSADVSGLAIKVPLSVDQSEDEGFQSAPNLTPDSQSEPGVTPDIDLWEAVLTYEASRRRCWEQIGCPPGHREEPYLTEAGRDAFDRFCRLRQGELQVLGGALLQAPQPVLVKESELVKDTLNVLLGVVSATFSLCQPAQAFTVKRGVHVSGASPESVSSLLSEVAECGTHYARLSDFSLQPVLDSSCSKGLVFQAFTSGLRRYLQYYRACVLSTPPTLSLLTIGFLFKKLGRQLRYLAELCGVGTALPGTGGGEPRAAFPTGVRLLSYLYQEALDNCSNEHYPVLLSLLKTSCEPYTRFIHDWVYSGVFRDVYGEFMIQVNHEYLGCRDKSYWTHGYVLVSKEVEACVPVFLKHVAHDVYVCGKTINLLKLCCPRHYLCCSDVPVPRISVIFSLEELKDIEKDCAIYVGRMERVARHSSLSKEEKELRMEIAKQELIVHAREAASRVLSALSDRQMSERMALDARKREQFQRLKEQFMRDQERRRAARQEELDDDFSYARELRDRERRLKALEEQLERKARQALVDHYSKLSAEAARRERKALWRVQRHRLADARRRFLLEEEKRVQVMPSCSWERNQGALVFQASLPCPEHPDGGGGCGSGPSEQPKAARDGPRGPSRLMPQLPESPAEAACGLLSVGLSIRDFLPTAQGAEQPLHTGSALVLEEALQTIGSDLPPPAPSAAVGTGPSGPQEYDFRTILRPAVATSAFPGPLQSTGGGLGSEGQPQWEDTHVQLDMCVLDGQVALPHACSPQKTSPQEGSQAMGQLLRQVSEGDVPTGGYASGTAPSRPRWNVHGHVSDASIKVGENVCDVVPSRPRWNVHGHVSDASIKVGENVCDVVPSRPRWNVHGHVSDASIKVGENVCDVVPSRPRWNIHGHVSDASIKVGENVCDVVPSRPRWNVHGHVSQSQVTLGVLSGEAEPIVPWPHQTPPDHGSQSGLSLGAQSPAQEGEPQPAAETAVEGAESGPQASPTAGAGSSLLSGSRLGPEARPPPPPPHLFCPGRSEDTVDLPASCRPSSQVRGQGLGVGGESSAGCPSHPACPFMGNEGSVPGPGVDTQSSPGLGEEAAQRWGMEQAYLAGLAGQYRLEQYPDSYEAMSEPPVARLLHHGLPRAFALPEDSGVQPDTDETAVQLSELLPLPVLMKHSVTAPLAAHVSLVNKAAVDYFFVELHLGAHFEALRHFLLMEDGEFAQSLSDLLFEKLGAGQTPGELLSPLVLNSVLSKALQYSLHGDTPHAANLSFALKFLPEAFAPNAPDVLSCLELRYKVDWPLNIVVTEGCLSRYSGIFSFLLQLKLMMWTLKDVCFHLKRTARMSHVASSVQFRQLQLFKHEMQHFVKVIQGYIANQILHVTWCEFRARLASVGDLEEIQRAHAEYLHKAVFRGLLTEKAAPAMNIIHSLFSLVLKFRSQLISQPWGLAGGPHGAEHPNFALMQQSYSTFKYYSHFLFKVVSKLVNRGYQPHLEDFLLRINFNNYYQDA

来源 Source

来源生物 organism	Sus scrofa
通用名 common_name	pig
NCBI Class编号 ncbi_taxonomy_id	9823
宿主生物 host_organism	Sus scrofa

Entity 6 Entity 6 polymer

Description description	Mitotic spindle organizing protein 1
Molecular weight formula_weight	8285.5 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	P,Q,O

MAGNSGSGAAAAANLNAVRETMDVLLEISRILNTGLDMETLSICVRLCEQGINPEALSSVIKELRKATEALKAAENMTS

来源 Source

来源生物 organism	Sus scrofa
通用名 common_name	pig
NCBI Class编号 ncbi_taxonomy_id	9823
宿主生物 host_organism	Sus scrofa

Entity 7 Entity 7 polymer

Description description	Mitotic-spindle organizing protein 2A isoform X4
Molecular weight formula_weight	15920.3 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	V,W,X,Y

MAAPGAGPGPGAPPGLEAALQKLALRRKKVLSAEETELFELAQAAGGAMDPEVFKILVDLLKLNVAPLAVFQMLKSMCAGQRLASEPQDPVAVPLPTTSVPETRGRNRGSSALGGGPALAERSGREGSSQRMPRQPSATRLPKGGGPGKSPTRST

来源 Source

来源生物 organism	Sus scrofa
通用名 common_name	pig
NCBI Class编号 ncbi_taxonomy_id	9823
宿主生物 host_organism	Sus scrofa

Entity 8 Entity 8 polymer

Description description	Tubulin gamma chain
Molecular weight formula_weight	51135.6 kDa
Source method src_method	man
Copy count entity_count	14

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	a,b,c,d,e,f,g,h,i,j,k,l,m,n

MPREIITLQLGQCGNQIGFEFWKQLCAEHGISPEGIVEEFATEGTDRKDVFFYQADDEHYIPRAVLLDLEPRVIHSILNSPYAKLYNPENIYLSEHGGGAGNNWASGFSQGEKIHEDIFDIIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPNQDEMSDVVVQPYNSLLTLKRLTQNADCVVVLDNTALNRIATDRLHIQNPSFSQINQLVSTIMSASTTTLRYPGYMNNDLIGLIASLIPTPRLHFLMTGYTPLTTDQSVASVRKTTVLDVMRRLLQPKNVMVSTGRDRQTNHCYIAILNIIQGEVDPTQVHKSLQRIRERKLANFIPWGPASIQVALSRKSPYLPSAHRVSGLMMANHTSISSLFESSCQQYDKLRKREAFLEQFRKEDIFKENFDELDRSREVVQELIDEYHAATRPDYISWGTQEQ

来源 Source

来源生物 organism	Sus scrofa
通用名 common_name	pig
NCBI Class编号 ncbi_taxonomy_id	9823
宿主生物 host_organism	Sus scrofa

Entity 9 Entity 9 polymer

Description description	CDK5 regulatory subunit-associated protein 2
Molecular weight formula_weight	189905.8 kDa
Source method src_method	man
Copy count entity_count	10

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	o,q,r,s,t,v,u,w,x,p

MMDLVLEEDVTVPGTLSGCSGLVPSVPDDLDGINPNAGLGNGLLPNVSEETVSPTRARNMKDFENQITELKKENFNLKLRIYFLEERMQQEFHGPTEHIYKTNIELKVEVESLKRELQEREQLLIKASKAVESLAEAGGSEIQRVKEDARKKVQQVEDLLTKRILLLEKDVTAAQAELEKAFAGTETEKALRLRLESKLSEMKKMHEGDLAMALVLDEKDRLIEELKLSLKSKEALIQCLKEEKSQMACPDENVSSGELRGLCAAPREEKERETEAAQMEHQKERNSFEERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEGLITEKCSSQQPPGSKTIFSKEKKQSSDYEELIQVLKKEQDIYTHLVKSLQESDSINNLQAELNKIFALRKQLEQDVLSYQNLRKTLEEQISEIRRREESFSLYSDQTSYLSICLEENNRFQVEHFSQEELKKKVSDLIQLVKELYTDNQHLKKTIFDLSCMGFQGNGFPDRLASTEQTEEAKKSRLPILIKPSRSLGNMYRLPATQEVVTQLQSQILELQGELKEFKTCNKQLHQKLILAEAVMEGRPTPDKTLLNAQPPVGAAYQDSPGEQKGIKTTSSVWRDKEMDSDQQRSYEIDSEICPPDDLASLPSCKENPEDVLSPTSVATYLSSKSQPSAKVSVMGTDQSESINTSNETEYLKQKIHDLETELEGYQNFIFQLQKHSQCSEAIITVLCGTEGAQDGLSKPKNGSDGEEMTFSSLHQVRYVKHVKILGPLAPEMIDSRVLENLKQQLEEQEYKLQKEQNLNMQLFSEIHNLQNKFRDLSPPRYDSLVQSQARELSLQRQQIKDGHGICVISRQHMNTMIKAFEELLQASDVDYCVAEGFQEQLNQCAELLEKLEKLFLNGKSVGVEMNTQNELMERIEEDNLTYQHLLPESPEPSASHALSDYETSEKSFFSRDQKQDNETEKTSVMVNSFSQDLLMEHIQEIRTLRKRLEESIKTNEKLRKQLERQGSEFVQGSTSIFASGSELHSSLTSEIHFLRKQNQALNAMLIKGSRDKQKENDKLRESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQEVRCSGQELSRVQEEVKLRQQLLSQNDKLLQSLRVELKAYEKLDEEHRRLREASGEGWKGQDPFRDLHSLLMEIQALRLQLERSIETSSTLQSRLKEQLARGAEKAQEGALTLAVQAVSIPEVPLQPDKHDGDKYPMESDNSFDLFDSSQAVTPKSVSETPPLSGNDTDSLSCDSGSSATSTPCVSRLVTGHHLWASKNGRHVLGLIEDYEALLKQISQGQRLLAEMDIQTQEAPSSTSQELGTKGPHPAPLSKFVSSVSTAKLTLEEAYRRLKLLWRVSLPEDGQCPLHCEQIGEMKAEVTKLHKKLFEQEKKLQNTMKLLQLSKRQEKVIFDQLVVTHKILRKARGNLELRPGGAHPGTCSPSRPGS

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	Human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

▶

8. Citations (1)

▶

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	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	triclinic

Resolution resolution	6.80 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	16448

fit	/app/data/saxs_computation/g3/9g3y/9g3y.fit
pddf	/app/data/pr_computation/g3/9g3y/9g3y.pr.out
profile	/app/data/saxs_computation/g3/9g3y/9g3y.dat

Structure of the Native CMG-decorated gamma-Tubulin Ring Complex from Pig Brain

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

Gamma-tubulin complex component

State in the Current Structure

Other States of the Same Protein in the Database

Gamma-tubulin complex component 3

State in the Current Structure

Other States of the Same Protein in the Database

Gamma-tubulin complex component

State in the Current Structure

Other States of the Same Protein in the Database

Gamma-tubulin complex component

State in the Current Structure

Other States of the Same Protein in the Database

Tubulin gamma complex associated protein 6

State in the Current Structure

Other States of the Same Protein in the Database

Mitotic spindle organizing protein 1

State in the Current Structure

Other States of the Same Protein in the Database

Mitotic-spindle organizing protein 2A isoform X4

State in the Current Structure

Other States of the Same Protein in the Database

Tubulin gamma chain

State in the Current Structure

Other States of the Same Protein in the Database

CDK5 regulatory subunit-associated protein 2

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

Symmetry Symmetry

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (9)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 polymer

Polymer Polymer

来源 Source

Entity 5 Entity 5 polymer

Polymer Polymer

来源 Source

Entity 6 Entity 6 polymer

Polymer Polymer

来源 Source

Entity 7 Entity 7 polymer

Polymer Polymer

来源 Source

Entity 8 Entity 8 polymer

Polymer Polymer

来源 Source

Entity 9 Entity 9 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)