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1ced

THE STRUCTURE OF CYTOCHROME C6 FROM MONORAPHIDIUM BRAUNII, NMR, MINIMIZED AVERAGE STRUCTURE

Method: SOLUTION NMR Dmax: 33.6 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

CYTOCHROME C6

OrganismNot specified

UniProt Q09099

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–89 Not recorded HEM PROTOPORPHYRIN IX CONTAINING FE × 1 SOLUTION NMR mmCIF provides none of the parsed experimental conditions 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 1CED Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1A2S THE SOLUTION NMR STRUCTURE OF OXIDIZED CYTOCHROME C6 FROM THE GREEN ALGA MONORAPHIDIUM BRAUNII, MINIMIZED AVERAGE STRUCTURE Deposited 1998-01-10 Different ligand/ion Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–89（89 aa）
Not recorded HEC HEME C × 1 SOLUTION NMR
NMR measurement conditions pH 5；300 K
Resolution not provided
1CTJ CRYSTAL STRUCTURE OF CYTOCHROME C6 Deposited 1995-08-08 Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–89（89 aa）
Not recorded HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；pH 7.5
Resolution 1.10 Å R-free 0.188

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CYC6_MONBR
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； 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 1ced

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ced
Deposition date deposition_date1996-03-06
Structure title titleTHE STRUCTURE OF CYTOCHROME C6 FROM MONORAPHIDIUM BRAUNII, NMR, MINIMIZED AVERAGE STRUCTURE
Keywords keywordsELECTRON TRANSPORT, HEME PROTEIN, CHLOROPLAST, THYLAKOID MEMBRANE, ELECTRON TRANSPORT (HEME PROTEIN); ELECTRON TRANSPORT (HEME PROTEIN)
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier11.68 Å
Radius of gyration Rg (electron density) rg_electron11.43 Å
Forward intensity I(0) i0578297000.00
Molecular weight molecular_weight199200.0 kDa
Excluded volume excluded_volume245900 ų
Envelope volume envelope_volume15178 ų
Hydration-shell volume shell_volume10546 ų
Envelope diameter envelope_diameter40.3 Å
Shell Rg shell_rg18.03 Å
Envelope Rg envelope_rg12.47 Å
Shape Rg shape_rg11.42 Å
Total Rg total_rg11.54 Å
Total atoms total_atoms14040
Residues n_residues1780
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax33.6 Å
Rg (real space) rg_real11.55 Å
Rg uncertainty (real space) rg_real_error0.17 Å
I(0) (real space) i0_real5.7830e+08
I(0) uncertainty (real space) i0_real_error5.3920e+06
Rg (reciprocal space) rg_reciprocal11.56 Å
I(0) (reciprocal space) i0_reciprocal578300000.0000
Solution quality estimate total_estimate0.8951
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.6 Å
Skewness Skewness skewness-0.097
Kurtosis Kurtosis kurtosis-0.397
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha157600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.923; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.964; Smooth: 0.898
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1ceda_
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 (1 domains)

Domain ID domain_id1cedA00
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
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8. Citations (3)

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9. Files and Curves (10)