1sh4

Solution structure of oxidized bovine microsomal cytochrome B5 Mutant V45H

Method: SOLUTION NMR Dmax: 36.8 Å Quality: EXCELLENT

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

Cytochrome b5

Bos taurus

UniProt P00171

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 7–88 Fragment:residues 3-84 Mutation:V45H HEM PROTOPORPHYRIN IX CONTAINING FE × 1 SOLUTION NMR NMR measurement conditions:pH 7;293 K;Ionic strength (raw mmCIF value) 25mM PHOSPHATE BUFFER;Pressure 1 NMR sample composition:3.0mM | 90% H2O/10% D2O NMR sample composition:3.0mM | 100% D2O 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.

19 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CYB5_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–82; UniProt 7–88

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 1sh4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1sh4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1sh4
Deposition date deposition_date2004-02-25
Structure title titleSolution structure of oxidized bovine microsomal cytochrome B5 Mutant V45H
Keywords keywordsFIVE HELIX, FIVE SHEET, HEME RING, ELECTRON TRANSPORT; ELECTRON TRANSPORT
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier12.35
Radius of gyration Rg (electron density) rg_electron12.11
Forward intensity I(0) i01290360000.00
Molecular weight molecular_weight302400.0 kDa
Excluded volume excluded_volume375160 ų
Envelope volume envelope_volume17902 ų
Hydration-shell volume shell_volume11489 ų
Envelope diameter envelope_diameter41.6
Shell Rg shell_rg18.98
Envelope Rg envelope_rg13.48
Shape Rg shape_rg12.08
Total Rg total_rg12.30
Total atoms total_atoms38130
Residues n_residues2460
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 dmax36.8
Rg (real space) rg_real12.26
Rg uncertainty (real space) rg_real_error0.22
I(0) (real space) i0_real1.2900e+09
I(0) uncertainty (real space) i0_real_error1.2420e+07
Rg (reciprocal space) rg_reciprocal12.26
I(0) (reciprocal space) i0_reciprocal1290000000.0000
Solution quality estimate total_estimate0.9076
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.4
Skewness Skewness skewness0.067
Kurtosis Kurtosis kurtosis-0.461
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha114600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.946; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.970

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_idd1sh4a_
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_id1sh4A00
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)