1bbh

ATOMIC STRUCTURE OF A CYTOCHROME C' WITH AN UNUSUAL LIGAND-CONTROLLED DIMER DISSOCIATION AT 1.8 ANGSTROMS RESOLUTION

Method: X-RAY DIFFRACTION Dmax: 60.6 Å Quality: EXCELLENT

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

;CYTOCHROME C' ;

Allochromatium vinosum

UniProt P00154

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 24–154 Chain B; UniProt 24–154 Not recorded HEC HEME C × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.80 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.

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

View Construct and Data Evidence
UniProt name CYCP_CHRVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–131; UniProt 24–154 Author chain B; PDBConstruct 1–131; UniProt 24–154

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 1bbh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1bbh
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1bbh
Deposition date deposition_date1992-05-18
Structure title titleATOMIC STRUCTURE OF A CYTOCHROME C' WITH AN UNUSUAL LIGAND-CONTROLLED DIMER DISSOCIATION AT 1.8 ANGSTROMS RESOLUTION
Keywords keywordsELECTRON TRANSPORT(HEME PROTEIN); ELECTRON TRANSPORT(HEME PROTEIN)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.55
Radius of gyration Rg (electron density) rg_electron18.45
Forward intensity I(0) i015414400.00
Molecular weight molecular_weight28812.0 kDa
Excluded volume excluded_volume35672 ų
Envelope volume envelope_volume41489 ų
Hydration-shell volume shell_volume18711 ų
Envelope diameter envelope_diameter61.0
Shell Rg shell_rg24.69
Envelope Rg envelope_rg18.68
Shape Rg shape_rg18.45
Total Rg total_rg19.33
Total atoms total_atoms2020
Residues n_residues262
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 dmax60.6
Rg (real space) rg_real19.39
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real1.5410e+07
I(0) uncertainty (real space) i0_real_error1.8330e+05
Rg (reciprocal space) rg_reciprocal19.42
I(0) (reciprocal space) i0_reciprocal15410000.0000
Solution quality estimate total_estimate0.9003
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.5
Skewness Skewness skewness0.054
Kurtosis Kurtosis kurtosis-0.540
Angular range angular_range— – 0.4050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3555000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.907; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.986

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_idd1bbha_
Class classa — All alpha proteins
Fold Fold folda.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamilya.24.3 — Cytochromes
Family Family familya.24.3.2 — Cytochrome c'-like
Domain ID domain_idd1bbhb_
Class classa — All alpha proteins
Fold Fold folda.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamilya.24.3 — Cytochromes
Family Family familya.24.3.2 — Cytochrome c'-like

CATH v4.4 (2 domains)

Domain ID domain_id1bbhA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily10 — Cytochrome c/b562
Domain ID domain_id1bbhB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily10 — Cytochrome c/b562

8. Citations (2)

9. Files and Curves (10)