2fwl

The cytochrome c552/CuA complex from Thermus thermophilus

Method: SOLUTION NMR Dmax: 72.2 Å Quality: GOOD

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

Cytochrome c-552

Thermus thermophilus

UniProt P04164

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–131 Not recorded Cytochrome c oxidase subunit II × 1 (P98052) HEC HEME C × 1 CUA DINUCLEAR COPPER ION × 1 SOLUTION NMR NMR measurement conditions:pH 6;298 K;Ionic strength (raw mmCIF value) 20mM phosphate buffer;Pressure ambient NMR sample composition:0.5mM cytochrome c552 U-15N, 20mM phosphate buffer, 2mM CuA domain, 95% H2O, 5% D2O | 95% H2O/5% D2O NMR sample composition:0.5mM CuA domain U-15N, 20mM phosphate buffer, 2mM cytochrome c552, 95% H2O, 5% D2O | 95% H2O/5% 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CY552_THETH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–133; UniProt 1–131

Cytochrome c oxidase subunit II

Thermus thermophilus

UniProt P98052

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–135 Not recorded Cytochrome c-552 × 1 (P04164) HEC HEME C × 1 CUA DINUCLEAR COPPER ION × 1 SOLUTION NMR NMR measurement conditions:pH 6;298 K;Ionic strength (raw mmCIF value) 20mM phosphate buffer;Pressure ambient NMR sample composition:0.5mM cytochrome c552 U-15N, 20mM phosphate buffer, 2mM CuA domain, 95% H2O, 5% D2O | 95% H2O/5% D2O NMR sample composition:0.5mM CuA domain U-15N, 20mM phosphate buffer, 2mM cytochrome c552, 95% H2O, 5% D2O | 95% H2O/5% 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.

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

View Construct and Data Evidence
UniProt name COX2_THETH
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–136; UniProt 1–135

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 2fwl

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2fwl
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2fwl
Deposition date deposition_date2006-02-02
Structure title titleThe cytochrome c552/CuA complex from Thermus thermophilus
Keywords keywordsdocking calculations, redox protein complex, electron transfer pathway, ELECTRON TRANSPORT-OXIDOREDUCTASE COMPLEX; ELECTRON TRANSPORT/OXIDOREDUCTASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier19.69
Radius of gyration Rg (electron density) rg_electron19.60
Forward intensity I(0) i0109130000.00
Molecular weight molecular_weight88367.0 kDa
Excluded volume excluded_volume111700 ų
Envelope volume envelope_volume49567 ų
Hydration-shell volume shell_volume20711 ų
Envelope diameter envelope_diameter75.5
Shell Rg shell_rg26.61
Envelope Rg envelope_rg20.72
Shape Rg shape_rg19.59
Total Rg total_rg20.04
Total atoms total_atoms12450
Residues n_residues789
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 dmax72.2
Rg (real space) rg_real19.76
Rg uncertainty (real space) rg_real_error0.61
I(0) (real space) i0_real1.0910e+08
I(0) uncertainty (real space) i0_real_error1.3470e+06
Rg (reciprocal space) rg_reciprocal19.75
I(0) (reciprocal space) i0_reciprocal109100000.0000
Solution quality estimate total_estimate0.8081
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.4
Skewness Skewness skewness0.508
Kurtosis Kurtosis kurtosis-0.034
Angular range angular_range— – 0.4050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3094000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.558; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.831; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2fwla_
Class classa — All alpha proteins
Fold Fold folda.3 — Cytochrome c
Superfamily Superfamily superfamilya.3.1 — Cytochrome c
Family Family familya.3.1.1 — monodomain cytochrome c
Domain ID domain_idd2fwlb_
Class classb — All beta proteins
Fold Fold foldb.6 — Cupredoxin-like
Superfamily Superfamily superfamilyb.6.1 — Cupredoxins
Family Family familyb.6.1.2 — Periplasmic domain of cytochrome c oxidase subunit II

CATH v4.4 (2 domains)

Domain ID domain_id2fwlA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily10 — Cytochrome c-like domain
Domain ID domain_id2fwlB02
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)