1l0m

Solution structure of Bacteriorhodopsin

Method: SOLUTION NMR Dmax: 59.8 Å Quality: REASONABLE

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

Bacteriorhodopsin

OrganismNot specified

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 20–231 Mutation:part of helix G absent No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6;293 K;Pressure 1 NMR sample composition:chmeically synthesized peptides | DMSO 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 1–212; UniProt 20–231

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 1l0m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1l0m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1l0m
Deposition date deposition_date2002-02-11
Structure title titleSolution structure of Bacteriorhodopsin
Keywords keywordsBacteriorhodopsin, alternative method for structure determination, PROTON TRANSPORT; PROTON TRANSPORT
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier18.25
Radius of gyration Rg (electron density) rg_electron17.30
Forward intensity I(0) i07750990.00
Molecular weight molecular_weight23226.0 kDa
Excluded volume excluded_volume30277 ų
Envelope volume envelope_volume34108 ų
Hydration-shell volume shell_volume16620 ų
Envelope diameter envelope_diameter61.1
Shell Rg shell_rg23.31
Envelope Rg envelope_rg17.59
Shape Rg shape_rg17.27
Total Rg total_rg18.50
Total atoms total_atoms3333
Residues n_residues212
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 dmax59.8
Rg (real space) rg_real18.18
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real7.7510e+06
I(0) uncertainty (real space) i0_real_error9.0410e+04
Rg (reciprocal space) rg_reciprocal18.20
I(0) (reciprocal space) i0_reciprocal7751000.0000
Solution quality estimate total_estimate0.7071
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.8
Skewness Skewness skewness0.227
Kurtosis Kurtosis kurtosis-0.369
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1086000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.865; Stabil: 1.000; Sysdev: 0.212; Positv: 1.000; Valcen: 1.000; Smooth: 0.959

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_idd1l0ma_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.13 — Class A G protein-coupled receptor (GPCR)-like
Superfamily Superfamily superfamilyf.13.1 — Class A G protein-coupled receptor (GPCR)-like
Family Family familyf.13.1.1 — Bacteriorhodopsin-like

CATH v4.4 (1 domains)

Domain ID domain_id1l0mA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1070 — Rhopdopsin 7-helix transmembrane proteins
Homologous superfamily homologous superfamily10 — Rhodopsin 7-helix transmembrane proteins

8. Citations (1)

9. Files and Curves (10)