1rcp

CYTOCHROME C'

Method: X-RAY DIFFRACTION Dmax: 72.2 Å Quality: GOOD

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

;CYTOCHROME C' ;

OrganismNot specified

UniProt P00147

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 22–150 Not recorded HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;pH 6.5 Resolution 2.00 Å
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 22–150 Not recorded HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;pH 6.5 Resolution 2.00 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.

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

View Construct and Data Evidence
UniProt name CYCP_RHOCA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–129; UniProt 22–150 Author chain B; PDBConstruct 1–129; UniProt 22–150

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 1rcp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1rcp
Deposition date deposition_date1995-08-23
Structure title titleCYTOCHROME C'
Keywords keywordsELECTRON TRANSPORT, CYTOCHROME, HEME; ELECTRON TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.73
Radius of gyration Rg (electron density) rg_electron20.94
Forward intensity I(0) i013871400.00
Molecular weight molecular_weight27431.0 kDa
Excluded volume excluded_volume34024 ų
Envelope volume envelope_volume40289 ų
Hydration-shell volume shell_volume17142 ų
Envelope diameter envelope_diameter71.3
Shell Rg shell_rg26.09
Envelope Rg envelope_rg21.00
Shape Rg shape_rg20.97
Total Rg total_rg21.55
Total atoms total_atoms2325
Residues n_residues258
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_real21.85
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real1.3870e+07
I(0) uncertainty (real space) i0_real_error1.8610e+05
Rg (reciprocal space) rg_reciprocal21.83
I(0) (reciprocal space) i0_reciprocal13870000.0000
Solution quality estimate total_estimate0.8688
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.5
Skewness Skewness skewness0.446
Kurtosis Kurtosis kurtosis-0.353
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6735000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.843; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.828; Smooth: 0.936

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_idd1rcpa_
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_idd1rcpb_
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_id1rcpA00
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_id1rcpB00
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 (1)

9. Files and Curves (10)