3mus

2A Resolution Structure of Rat Type B Cytochrome b5

Method: X-RAY DIFFRACTION Dmax: 63.1 Å Quality: REASONABLE

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

Cytochrome b5 type B

Rattus norvegicus

UniProt P04166

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 17–102 Fragment:UNP residues 17-102 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.8;277 K;30%PEG8K, 0.2M MgAc, 0.1M Hepes, pH 6.8, EVAPORATION, temperature 277K Resolution 2.00 Å R-free 0.223
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 17–102 Fragment:UNP residues 17-102 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.8;277 K;30%PEG8K, 0.2M MgAc, 0.1M Hepes, pH 6.8, EVAPORATION, temperature 277K Resolution 2.00 Å R-free 0.223

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.

7 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CYB5B_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–86; UniProt 17–102 Author chain B; PDBConstruct 1–86; UniProt 17–102

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 3mus

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3mus
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3mus
Deposition date deposition_date2010-05-03
Structure title title2A Resolution Structure of Rat Type B Cytochrome b5
Keywords keywordsCYTOCHROME b5, HEME, 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_guinier18.06
Radius of gyration Rg (electron density) rg_electron17.00
Forward intensity I(0) i08313670.00
Molecular weight molecular_weight20764.0 kDa
Excluded volume excluded_volume25711 ų
Envelope volume envelope_volume30701 ų
Hydration-shell volume shell_volume15520 ų
Envelope diameter envelope_diameter62.3
Shell Rg shell_rg22.59
Envelope Rg envelope_rg17.18
Shape Rg shape_rg16.98
Total Rg total_rg17.98
Total atoms total_atoms1466
Residues n_residues172
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 dmax63.1
Rg (real space) rg_real18.00
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real8.3140e+06
I(0) uncertainty (real space) i0_real_error1.1790e+05
Rg (reciprocal space) rg_reciprocal18.00
I(0) (reciprocal space) i0_reciprocal8314000.0000
Solution quality estimate total_estimate0.6466
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary57.2
Skewness Skewness skewness0.255
Kurtosis Kurtosis kurtosis-0.363
Angular range angular_range— – 0.4400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2796000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.730; Stabil: 1.000; Sysdev: 0.408; Positv: 1.000; Valcen: 0.988; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd3musa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.120 — Cytochrome b5-like heme/steroid binding domain
Superfamily Superfamily superfamilyd.120.1 — Cytochrome b5-like heme/steroid binding domain
Family Family familyd.120.1.1 — Cytochrome b5
Domain ID domain_idd3musb1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.120 — Cytochrome b5-like heme/steroid binding domain
Superfamily Superfamily superfamilyd.120.1 — Cytochrome b5-like heme/steroid binding domain
Family Family familyd.120.1.1 — Cytochrome b5
Domain ID domain_idd3musb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id3musA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology120 — Flavocytochrome B2; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Cytochrome b5-like heme/steroid binding domain
Domain ID domain_id3musB00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology120 — Flavocytochrome B2; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Cytochrome b5-like heme/steroid binding domain

8. Citations (1)

9. Files and Curves (10)