8hua

Serial synchrotron crystallography structure of ba3-type cytochrome c oxidase from Thermus thermophilus using a goniometer compatible flow-cell

Method: X-RAY DIFFRACTION Dmax: 88.8 Å Quality: GOOD

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

Cytochrome c oxidase subunit 1

Thermus thermophilus

UniProt Q5SJ79

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 2–562 Not recorded Cytochrome c oxidase subunit 2 × 1 (Q5SJ80) Cytochrome c oxidase polypeptide 2A × 1 (P82543) CU COPPER (II) ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 HAS HEME-AS × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 15 CUA DINUCLEAR COPPER ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;pH 5.3;298 K;1.4 M NaCl, 100 mM MES pH 5.3 with 36 % to 39 % (v/v) PEG 400 Resolution 2.12 Å R-free 0.184

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.

40 other PDB entries and 43 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX1_THET8
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 9–569; UniProt 2–562

Cytochrome c oxidase subunit 2

Thermus thermophilus HB8

UniProt Q5SJ80

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–168 Not recorded Cytochrome c oxidase subunit 1 × 1 (Q5SJ79) Cytochrome c oxidase polypeptide 2A × 1 (P82543) CU COPPER (II) ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 HAS HEME-AS × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 15 CUA DINUCLEAR COPPER ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;pH 5.3;298 K;1.4 M NaCl, 100 mM MES pH 5.3 with 36 % to 39 % (v/v) PEG 400 Resolution 2.12 Å R-free 0.184

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.

40 other PDB entries and 43 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX2_THET8
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–168; UniProt 1–168

Cytochrome c oxidase polypeptide 2A

Thermus thermophilus HB8

UniProt P82543

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–34 Not recorded Cytochrome c oxidase subunit 1 × 1 (Q5SJ79) Cytochrome c oxidase subunit 2 × 1 (Q5SJ80) CU COPPER (II) ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 HAS HEME-AS × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 15 CUA DINUCLEAR COPPER ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;pH 5.3;298 K;1.4 M NaCl, 100 mM MES pH 5.3 with 36 % to 39 % (v/v) PEG 400 Resolution 2.12 Å R-free 0.184

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.

39 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COXA_THET8
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–34; UniProt 1–34

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 8hua

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8hua
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8hua
Deposition date deposition_date2022-12-22
Structure title titleSerial synchrotron crystallography structure of ba3-type cytochrome c oxidase from Thermus thermophilus using a goniometer compatible flow-cell
Keywords keywordsMembrane protein, bioenergetics, serial crystallography, lipidic cubic phase, flow-cell, sample delivery system, ELECTRON TRANSPORT; ELECTRON TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.33
Radius of gyration Rg (electron density) rg_electron26.02
Forward intensity I(0) i091708100.00
Molecular weight molecular_weight88818.0 kDa
Excluded volume excluded_volume116580 ų
Envelope volume envelope_volume129430 ų
Hydration-shell volume shell_volume39353 ų
Envelope diameter envelope_diameter90.5
Shell Rg shell_rg35.17
Envelope Rg envelope_rg26.49
Shape Rg shape_rg26.00
Total Rg total_rg27.11
Total atoms total_atoms6294
Residues n_residues752
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 dmax88.8
Rg (real space) rg_real27.26
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real9.1710e+07
I(0) uncertainty (real space) i0_real_error1.2150e+06
Rg (reciprocal space) rg_reciprocal27.28
I(0) (reciprocal space) i0_reciprocal91710000.0000
Solution quality estimate total_estimate0.8883
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.2
Skewness Skewness skewness0.317
Kurtosis Kurtosis kurtosis-0.306
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24320000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.859; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.968

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id8huaA01
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

8. Citations (1)

9. Files and Curves (10)