1c6o

CRYSTAL STRUCTURE OF OXIDIZED CYTOCHROME C6 FROM THE GREEN ALGAE SCENEDESMUS OBLIQUUS

Method: X-RAY DIFFRACTION Dmax: 62.0 Å Quality: GOOD

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

CYTOCHROME C6

OrganismNot specified

UniProt P57736

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 1–89 Chain B; UniProt 1–89 Not recorded HEM PROTOPORPHYRIN IX CONTAINING FE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;pH 8.5 Resolution 2.00 Å R-free 0.279

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.

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

View Construct and Data Evidence
UniProt name CYC6_SCEOB
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–89; UniProt 1–89 Author chain B; PDBConstruct 1–89; UniProt 1–89

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 1c6o

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1c6o
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1c6o
Deposition date deposition_date1999-04-07
Structure title titleCRYSTAL STRUCTURE OF OXIDIZED CYTOCHROME C6 FROM THE GREEN ALGAE SCENEDESMUS OBLIQUUS
Keywords keywordsELECTRON TRANSPORT PROTEIN, CYTOCHROME-C6, OXIDIZED STATE, PHOTOSYNTHESIS, DIMERIZATION, 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_guinier18.76
Radius of gyration Rg (electron density) rg_electron18.12
Forward intensity I(0) i07857540.00
Molecular weight molecular_weight20036.0 kDa
Excluded volume excluded_volume24637 ų
Envelope volume envelope_volume27983 ų
Hydration-shell volume shell_volume13733 ų
Envelope diameter envelope_diameter62.3
Shell Rg shell_rg22.82
Envelope Rg envelope_rg18.23
Shape Rg shape_rg18.13
Total Rg total_rg18.80
Total atoms total_atoms1408
Residues n_residues178
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 dmax62.0
Rg (real space) rg_real18.83
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real7.8580e+06
I(0) uncertainty (real space) i0_real_error9.0690e+04
Rg (reciprocal space) rg_reciprocal18.82
I(0) (reciprocal space) i0_reciprocal7858000.0000
Solution quality estimate total_estimate0.8662
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.7
Skewness Skewness skewness0.408
Kurtosis Kurtosis kurtosis-0.483
Angular range angular_range— – 0.4250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2621000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.794; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.910; Smooth: 0.964

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1c6oa_
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_idd1c6ob_
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

CATH v4.4 (2 domains)

Domain ID domain_id1c6oA00
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_id1c6oB00
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

8. Citations (1)

9. Files and Curves (10)