7z10

Monomeric respiratory complex IV isolated from S. cerevisiae

Method: ELECTRON MICROSCOPY Dmax: 121.8 Å Quality: GOOD

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

Cytochrome c oxidase subunit 1

OrganismNot specified

UniProt P00401

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain a; UniProt 1–534 Not recorded Cytochrome c oxidase subunit 2 × 1 (P00410) CYTOCHROME C OXIDASE SUBUNIT 3; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE III, COX3 × 1 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 1 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 1 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 1 (P00427) CYTOCHROME C OXIDASE SUBUNIT 7; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VII, COX7 × 1 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 1 (P04039) CYTOCHROME C OXIDASE SUBUNIT 7A; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIIA, COX9 × 1 (P07255) CU COPPER (II) ION × 1 HEA HEME-A × 2 MG MAGNESIUM ION × 1 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 3 CUA DINUCLEAR COPPER ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microliters of sample applied to negatively glow discharged grig. Resolution 3.87 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.

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain a; PDBConstruct 1–534; UniProt 1–534

Cytochrome c oxidase subunit 2

Saccharomyces cerevisiae S288C

UniProt P00410

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain b; UniProt 16–251 Not recorded Cytochrome c oxidase subunit 1 × 1 (P00401) CYTOCHROME C OXIDASE SUBUNIT 3; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE III, COX3 × 1 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 1 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 1 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 1 (P00427) CYTOCHROME C OXIDASE SUBUNIT 7; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VII, COX7 × 1 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 1 (P04039) CYTOCHROME C OXIDASE SUBUNIT 7A; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIIA, COX9 × 1 (P07255) CU COPPER (II) ION × 1 HEA HEME-A × 2 MG MAGNESIUM ION × 1 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 3 CUA DINUCLEAR COPPER ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microliters of sample applied to negatively glow discharged grig. Resolution 3.87 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX2_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain b; PDBConstruct 1–236; UniProt 16–251

CYTOCHROME C OXIDASE SUBUNIT 3; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE III, COX3

Saccharomyces cerevisiae S288C

UniProt P00420

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain c; UniProt 1–269 Not recorded Cytochrome c oxidase subunit 1 × 1 (P00401) Cytochrome c oxidase subunit 2 × 1 (P00410) Cytochrome c oxidase subunit 4, mitochondrial × 1 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 1 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 1 (P00427) CYTOCHROME C OXIDASE SUBUNIT 7; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VII, COX7 × 1 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 1 (P04039) CYTOCHROME C OXIDASE SUBUNIT 7A; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIIA, COX9 × 1 (P07255) CU COPPER (II) ION × 1 HEA HEME-A × 2 MG MAGNESIUM ION × 1 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 3 CUA DINUCLEAR COPPER ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microliters of sample applied to negatively glow discharged grig. Resolution 3.87 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX3_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain c; PDBConstruct 1–269; UniProt 1–269

Cytochrome c oxidase subunit 4, mitochondrial

Saccharomyces cerevisiae S288C

UniProt P04037

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain d; UniProt 29–149 Not recorded Cytochrome c oxidase subunit 1 × 1 (P00401) Cytochrome c oxidase subunit 2 × 1 (P00410) CYTOCHROME C OXIDASE SUBUNIT 3; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE III, COX3 × 1 (P00420) Cytochrome c oxidase polypeptide 5A, mitochondrial × 1 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 1 (P00427) CYTOCHROME C OXIDASE SUBUNIT 7; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VII, COX7 × 1 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 1 (P04039) CYTOCHROME C OXIDASE SUBUNIT 7A; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIIA, COX9 × 1 (P07255) CU COPPER (II) ION × 1 HEA HEME-A × 2 MG MAGNESIUM ION × 1 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 3 CUA DINUCLEAR COPPER ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microliters of sample applied to negatively glow discharged grig. Resolution 3.87 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.

12 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX4_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain d; PDBConstruct 1–121; UniProt 29–149

Cytochrome c oxidase polypeptide 5A, mitochondrial

Saccharomyces cerevisiae S288C

UniProt P00424

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain e; UniProt 21–153 Not recorded Cytochrome c oxidase subunit 1 × 1 (P00401) Cytochrome c oxidase subunit 2 × 1 (P00410) CYTOCHROME C OXIDASE SUBUNIT 3; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE III, COX3 × 1 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 1 (P04037) Cytochrome c oxidase subunit 6, mitochondrial × 1 (P00427) CYTOCHROME C OXIDASE SUBUNIT 7; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VII, COX7 × 1 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 1 (P04039) CYTOCHROME C OXIDASE SUBUNIT 7A; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIIA, COX9 × 1 (P07255) CU COPPER (II) ION × 1 HEA HEME-A × 2 MG MAGNESIUM ION × 1 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 3 CUA DINUCLEAR COPPER ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microliters of sample applied to negatively glow discharged grig. Resolution 3.87 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.

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

View Construct and Data Evidence
UniProt name COX5A_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain e; PDBConstruct 1–133; UniProt 21–153

Cytochrome c oxidase subunit 6, mitochondrial

Saccharomyces cerevisiae S288C

UniProt P00427

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain f; UniProt 45–148 Not recorded Cytochrome c oxidase subunit 1 × 1 (P00401) Cytochrome c oxidase subunit 2 × 1 (P00410) CYTOCHROME C OXIDASE SUBUNIT 3; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE III, COX3 × 1 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 1 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 1 (P00424) CYTOCHROME C OXIDASE SUBUNIT 7; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VII, COX7 × 1 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 1 (P04039) CYTOCHROME C OXIDASE SUBUNIT 7A; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIIA, COX9 × 1 (P07255) CU COPPER (II) ION × 1 HEA HEME-A × 2 MG MAGNESIUM ION × 1 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 3 CUA DINUCLEAR COPPER ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microliters of sample applied to negatively glow discharged grig. Resolution 3.87 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX6_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain f; PDBConstruct 1–104; UniProt 45–148

CYTOCHROME C OXIDASE SUBUNIT 7; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VII, COX7

Saccharomyces cerevisiae S288C

UniProt P10174

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain g; UniProt 2–60 Not recorded Cytochrome c oxidase subunit 1 × 1 (P00401) Cytochrome c oxidase subunit 2 × 1 (P00410) CYTOCHROME C OXIDASE SUBUNIT 3; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE III, COX3 × 1 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 1 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 1 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 1 (P00427) Cytochrome c oxidase polypeptide VIII, mitochondrial × 1 (P04039) CYTOCHROME C OXIDASE SUBUNIT 7A; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIIA, COX9 × 1 (P07255) CU COPPER (II) ION × 1 HEA HEME-A × 2 MG MAGNESIUM ION × 1 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 3 CUA DINUCLEAR COPPER ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microliters of sample applied to negatively glow discharged grig. Resolution 3.87 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX7_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain g; PDBConstruct 1–59; UniProt 2–60

Cytochrome c oxidase polypeptide VIII, mitochondrial

Saccharomyces cerevisiae S288C

UniProt P04039

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain h; UniProt 28–74 Not recorded Cytochrome c oxidase subunit 1 × 1 (P00401) Cytochrome c oxidase subunit 2 × 1 (P00410) CYTOCHROME C OXIDASE SUBUNIT 3; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE III, COX3 × 1 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 1 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 1 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 1 (P00427) CYTOCHROME C OXIDASE SUBUNIT 7; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VII, COX7 × 1 (P10174) CYTOCHROME C OXIDASE SUBUNIT 7A; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIIA, COX9 × 1 (P07255) CU COPPER (II) ION × 1 HEA HEME-A × 2 MG MAGNESIUM ION × 1 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 3 CUA DINUCLEAR COPPER ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microliters of sample applied to negatively glow discharged grig. Resolution 3.87 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX8_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain h; PDBConstruct 1–47; UniProt 28–74

CYTOCHROME C OXIDASE SUBUNIT 7A; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIIA, COX9

Saccharomyces cerevisiae S288C

UniProt P07255

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain i; UniProt 2–56 Not recorded Cytochrome c oxidase subunit 1 × 1 (P00401) Cytochrome c oxidase subunit 2 × 1 (P00410) CYTOCHROME C OXIDASE SUBUNIT 3; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE III, COX3 × 1 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 1 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 1 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 1 (P00427) CYTOCHROME C OXIDASE SUBUNIT 7; SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VII, COX7 × 1 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 1 (P04039) CU COPPER (II) ION × 1 HEA HEME-A × 2 MG MAGNESIUM ION × 1 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 3 CUA DINUCLEAR COPPER ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microliters of sample applied to negatively glow discharged grig. Resolution 3.87 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX9_YEAST
Isoform
PDB entities 9
Chains and sequence ranges Author chain i; PDBConstruct 1–55; UniProt 2–56

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 7z10

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7z10
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7z10
Deposition date deposition_date2022-02-24
Structure title titleMonomeric respiratory complex IV isolated from S. cerevisiae
Keywords keywordsCytochrome C Oxidase, Mitochondria Respiratory Chain, Complex IV, Oxidoreductace-electron transport complex, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.58
Radius of gyration Rg (electron density) rg_electron36.41
Forward intensity I(0) i0405111000.00
Molecular weight molecular_weight178120.0 kDa
Excluded volume excluded_volume228430 ų
Envelope volume envelope_volume281470 ų
Hydration-shell volume shell_volume62024 ų
Envelope diameter envelope_diameter130.6
Shell Rg shell_rg44.17
Envelope Rg envelope_rg36.93
Shape Rg shape_rg36.40
Total Rg total_rg36.95
Total atoms total_atoms12574
Residues n_residues1556
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax121.8
Rg (real space) rg_real37.49
Rg uncertainty (real space) rg_real_error1.18
I(0) (real space) i0_real4.0510e+08
I(0) uncertainty (real space) i0_real_error6.4280e+06
Rg (reciprocal space) rg_reciprocal37.55
I(0) (reciprocal space) i0_reciprocal405100000.0000
Solution quality estimate total_estimate0.8978
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary43.5
Skewness Skewness skewness0.250
Kurtosis Kurtosis kurtosis-0.503
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha93340000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.910; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.942

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (15)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id7z10a01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology210 — Cytochrome C Oxidase; Chain A
Homologous superfamily homologous superfamily10 — Cytochrome c oxidase-like, subunit I domain
Domain ID domain_id7z10b01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily90
Domain ID domain_id7z10b02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins

8. Citations (1)

9. Files and Curves (10)