SAXSdb — 6zdb

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

Cytochrome c oxidase subunit 13, mitochondrial

Saccharomyces cerevisiae S288C

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–129 Chain B； UniProt 1–129	Not recorded	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 6.5；313.15 K；Ionic strength (raw mmCIF value) 20；Pressure 1 NMR sample composition：0.5 mM [U-15N] Cytochrome c oxidase subunit 13, Cox13, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition：0.5 mM [U-13C; U-15N] Cytochrome c oxidase subunit 13, Cox13, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition：0.5 mM 50%[15N, 13C] mixed with 50% [14N, 12C] Cytochrome c oxidase subunit 13, Cox13, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided

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 6ZDB	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6HU9 III2-IV2 mitochondrial respiratory supercomplex from S. cerevisiae Deposited 2018-10-05	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 44 PDB declaration: 44-meric	Chain k 10–129（120 aa） Chain w 10–129（120 aa）	Not recorded	PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 28 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 1 CDL CARDIOLIPIN × 8 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 4 ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE；3 microL of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec	Resolution 3.35 Å
6T0B The III2-IV(5B)2 respiratory supercomplex from S. cerevisiae Deposited 2019-10-02	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 46 PDB declaration: 46-meric	Chain k 10–129（120 aa） Chain x 10–129（120 aa）	Not recorded	CDL CARDIOLIPIN × 8 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 26 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 7 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE；3 microliter of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 s	Resolution 2.80 Å
6T15 The III2-IV(5B)1 respiratory supercomplex from S. cerevisiae Deposited 2019-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 33 PDB declaration: 33-meric	Chain k 10–129（120 aa）	Not recorded	PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 18 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 CDL CARDIOLIPIN × 7 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 1 HEA HEME-A × 2 MG MAGNESIUM ION × 1 CUA DINUCLEAR COPPER ION × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE；3 microliter of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 s	Resolution 3.29 Å
6YMX CIII2/CIV respiratory supercomplex from Saccharomyces cerevisiae Deposited 2020-04-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 32 PDB declaration: 32-meric	Chain k 16–129（114 aa）	Not recorded	CU COPPER (II) ION × 1 HEA HEME-A × 2 PTY PHOSPHATIDYLETHANOLAMINE × 7 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 CUA DINUCLEAR COPPER ION × 1 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 5 ZN ZINC ION × 1 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.17 Å
6YMY Cytochrome c oxidase from Saccharomyces cerevisiae Deposited 2020-04-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain k 16–129（114 aa）	Not recorded	CU COPPER (II) ION × 1 HEA HEME-A × 2 PTY PHOSPHATIDYLETHANOLAMINE × 7 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 CUA DINUCLEAR COPPER ION × 1 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 3 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.41 Å
8E7S III2IV2 respiratory supercomplex from Saccharomyces cerevisiae with 4 bound UQ6 Deposited 2022-08-24	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 44 PDB declaration: 44-meric	Chain S 1–129（129 aa） Chain s 1–129（129 aa）	Not recorded	PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 24 FES FE2/S2 (INORGANIC) CLUSTER × 2 CDL CARDIOLIPIN × 10 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 4 HEA HEME-A × 4 CU COPPER (II) ION × 2 CUA DINUCLEAR COPPER ION × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8EC0 III2IV respiratory supercomplex from Saccharomyces cerevisiae cardiolipin-lacking mutant Deposited 2022-08-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-meric	Chain S 1–129（129 aa）	Not recorded	PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 15 PGT (1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE × 7 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 CU COPPER (II) ION × 1 HEA HEME-A × 2 CUA DINUCLEAR COPPER ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
9BPB Tethered respiratory III2IV2 supercomplex from Saccharomyces cerevisiae Deposited 2024-05-07	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 42 PDB declaration: 42-meric	Chain k 1–129（129 aa） Chain w 1–129（129 aa）	Not recorded	CDL CARDIOLIPIN × 8 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 PTY PHOSPHATIDYLETHANOLAMINE × 10 HEA HEME-A × 4 CU COPPER (II) ION × 2 CA CALCIUM ION × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE；3 uL of sample, 5 s blot time, 30 s hold time, 0 blot force.	Resolution 2.57 Å
9ETZ III2IV respiratory supercomplex from Saccharomyces cerevisiae Deposited 2024-03-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 32 PDB declaration: 32-meric	Chain k 13–125（113 aa）	Not recorded	CDL CARDIOLIPIN × 11 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 26 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 6 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 1 HEA HEME-A × 2 CA CALCIUM ION × 1 MG MAGNESIUM ION × 1 CUA DINUCLEAR COPPER ION × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.40 Å

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	COX13_YEAST
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–129； UniProt 1–129 Author chain B； PDBConstruct 1–129； UniProt 1–129

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	6zdb
Deposition date deposition_date	2020-06-14
Structure title title	NMR structural analysis of yeast Cox13 reveals its C-terminus in interaction with ATP
Keywords keywords	membrane protein, solution structure, ATP/ADP, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	46.82 Å
Radius of gyration Rg (electron density) rg_electron	46.87 Å
Forward intensity I(0) i0	2752450000.00
Molecular weight molecular_weight	450170.0 kDa
Excluded volume excluded_volume	564900 Å³
Envelope volume envelope_volume	551660 Å³
Hydration-shell volume shell_volume	82101 Å³
Envelope diameter envelope_diameter	193.3 Å
Shell Rg shell_rg	58.83 Å
Envelope Rg envelope_rg	54.96 Å
Shape Rg shape_rg	46.80 Å
Total Rg total_rg	47.38 Å
Total atoms total_atoms	62940
Residues n_residues	3870
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	174.1 Å
Rg (real space) rg_real	47.42 Å
Rg uncertainty (real space) rg_real_error	3.02 Å
I(0) (real space) i0_real	2.7520e+09
I(0) uncertainty (real space) i0_real_error	6.2760e+07
Rg (reciprocal space) rg_reciprocal	46.82 Å
I(0) (reciprocal space) i0_reciprocal	2750000000.0000
Solution quality estimate total_estimate	0.7359
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	41.0 Å
Skewness Skewness skewness	0.521
Kurtosis Kurtosis kurtosis	-0.321
Angular range angular_range	— – 0.1700 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	9626000.0000
Real-space data points n_real_points	35
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.597; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.775; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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Description description	Cytochrome c oxidase subunit 13, mitochondrial
Molecular weight formula_weight	15046.1 kDa
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	62940

来源生物 organism	Saccharomyces cerevisiae S288C
NCBI Class编号 ncbi_taxonomy_id	559292
宿主生物 host_organism	Escherichia coli K-12

fit	/app/data/saxs_computation/zd/6zdb/6zdb.fit
pddf	/app/data/pr_computation/zd/6zdb/6zdb.pr.out
profile	/app/data/saxs_computation/zd/6zdb/6zdb.dat

NMR structural analysis of yeast Cox13 reveals its C-terminus in interaction with ATP

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

Cytochrome c oxidase subunit 13, mitochondrial

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

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)