1bct

THREE-DIMENSIONAL STRUCTURE OF PROTEOLYTIC FRAGMENT 163-231 OF BACTERIOOPSIN DETERMINED FROM NUCLEAR MAGNETIC RESONANCE DATA IN SOLUTION

Method: SOLUTION NMR Dmax: 109.2 Å Quality: REASONABLE

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

BACTERIORHODOPSIN

Halobacterium salinarum

UniProt P02945

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 176–244 Not recorded No other associated polymer SOLUTION NMR mmCIF provides none of the parsed experimental conditions 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.

173 other PDB entries and 201 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BACR_HALN1
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–69; UniProt 176–244

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 1bct

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1bct
Deposition date deposition_date1993-07-07
Structure title titleTHREE-DIMENSIONAL STRUCTURE OF PROTEOLYTIC FRAGMENT 163-231 OF BACTERIOOPSIN DETERMINED FROM NUCLEAR MAGNETIC RESONANCE DATA IN SOLUTION
Keywords keywordsPHOTORECEPTOR; PHOTORECEPTOR
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier28.57
Radius of gyration Rg (electron density) rg_electron28.25
Forward intensity I(0) i0127587000.00
Molecular weight molecular_weight105480.0 kDa
Excluded volume excluded_volume137800 ų
Envelope volume envelope_volume111560 ų
Hydration-shell volume shell_volume28694 ų
Envelope diameter envelope_diameter112.8
Shell Rg shell_rg37.25
Envelope Rg envelope_rg35.93
Shape Rg shape_rg28.20
Total Rg total_rg29.04
Total atoms total_atoms15442
Residues n_residues966
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 dmax109.2
Rg (real space) rg_real29.08
Rg uncertainty (real space) rg_real_error1.70
I(0) (real space) i0_real1.2760e+08
I(0) uncertainty (real space) i0_real_error2.4220e+06
Rg (reciprocal space) rg_reciprocal28.92
I(0) (reciprocal space) i0_reciprocal127600000.0000
Solution quality estimate total_estimate0.6862
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks4
Primary peak position r_peak_primary27.3
Skewness Skewness skewness0.433
Kurtosis Kurtosis kurtosis-0.223
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha111200.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.183; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.420; Smooth: 0.946

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1bcta_
Class classj — Peptides
Fold Fold foldj.35 — Transmembrane helical fragments
Superfamily Superfamily superfamilyj.35.1 — Transmembrane helical fragments
Family Family familyj.35.1.1 — Transmembrane helical fragments

CATH v4.4 (1 domains)

Domain ID domain_id1bctA00
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology290 — Bacteriorhodopsin Fragment
Homologous superfamily homologous superfamily10 — Bacteriorhodopsin Fragment

8. Citations (2)

9. Files and Curves (10)