1b5m

RAT OUTER MITOCHONDRIAL MEMBRANE CYTOCHROME B5

Method: X-RAY DIFFRACTION Dmax: 43.2 Å Quality: REASONABLE

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

CYTOCHROME B5

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 19–102 Fragment:WATER SOLUBLE DOMAIN HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:vapor diffusion with slow evaporation;pH 6.5;CRYSTALS WERE OBTAINED BY VAPOR DIFFUSION TOGETHER WITH SLOW EVAPORATION USING 20% PEG 8000 IN 0.1M SODIUM CACODYLATE (PH = 6.5 WITH 0.2 M MAGNESIUM ACETATE., vapor diffusion with slow evaporation Resolution 2.70 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.

7 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CYM5_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–84; UniProt 19–102

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 1b5m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1b5m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1b5m
Deposition date deposition_date1996-11-07
Structure title titleRAT OUTER MITOCHONDRIAL MEMBRANE CYTOCHROME B5
Keywords keywordsCYTOCHROME, ELECTRON TRANSPORT, HEME; ELECTRON TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier13.73
Radius of gyration Rg (electron density) rg_electron12.35
Forward intensity I(0) i02262760.00
Molecular weight molecular_weight10184.0 kDa
Excluded volume excluded_volume12617 ų
Envelope volume envelope_volume13835 ų
Hydration-shell volume shell_volume9732 ų
Envelope diameter envelope_diameter41.0
Shell Rg shell_rg17.83
Envelope Rg envelope_rg12.72
Shape Rg shape_rg12.34
Total Rg total_rg13.66
Total atoms total_atoms719
Residues n_residues84
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 dmax43.2
Rg (real space) rg_real13.65
Rg uncertainty (real space) rg_real_error0.24
I(0) (real space) i0_real2.2630e+06
I(0) uncertainty (real space) i0_real_error2.4380e+04
Rg (reciprocal space) rg_reciprocal13.66
I(0) (reciprocal space) i0_reciprocal2263000.0000
Solution quality estimate total_estimate0.7447
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.4
Skewness Skewness skewness0.161
Kurtosis Kurtosis kurtosis-0.336
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha349800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.876; Stabil: 1.000; Sysdev: 0.368; Positv: 1.000; Valcen: 0.993; Smooth: 0.951

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1b5ma_
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

CATH v4.4 (1 domains)

Domain ID domain_id1b5mA00
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)