1s51

Thr24Ser Bacteriorhodopsin

Method: X-RAY DIFFRACTION Dmax: 80.5 Å Quality: EXCELLENT

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 18–244 Mutation:T24S RET RETINAL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:bicelle vapor diffusion hanging drop;pH 3.7;310 K;sodium phosphate, hexanediol, pH 3.7, bicelle vapor diffusion hanging drop, temperature 310K Resolution 2.00 Å R-free 0.272
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 18–244 Mutation:T24S RET RETINAL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:bicelle vapor diffusion hanging drop;pH 3.7;310 K;sodium phosphate, hexanediol, pH 3.7, bicelle vapor diffusion hanging drop, temperature 310K Resolution 2.00 Å R-free 0.272

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 200 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 1–227; UniProt 18–244 Author chain B; PDBConstruct 1–227; UniProt 18–244

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 1s51

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1s51
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1s51
Deposition date deposition_date2004-01-19
Structure title titleThr24Ser Bacteriorhodopsin
Keywords keywordsmembrane protein; bacteriorhodopsin, PROTON TRANSPORT; PROTON TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.96
Radius of gyration Rg (electron density) rg_electron23.83
Forward intensity I(0) i031591900.00
Molecular weight molecular_weight50204.0 kDa
Excluded volume excluded_volume65681 ų
Envelope volume envelope_volume73344 ų
Hydration-shell volume shell_volume25619 ų
Envelope diameter envelope_diameter81.3
Shell Rg shell_rg30.93
Envelope Rg envelope_rg23.88
Shape Rg shape_rg23.84
Total Rg total_rg24.74
Total atoms total_atoms3552
Residues n_residues454
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 dmax80.5
Rg (real space) rg_real24.86
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real3.1590e+07
I(0) uncertainty (real space) i0_real_error4.3600e+05
Rg (reciprocal space) rg_reciprocal24.89
I(0) (reciprocal space) i0_reciprocal31590000.0000
Solution quality estimate total_estimate0.9049
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary79.2
Skewness Skewness skewness0.164
Kurtosis Kurtosis kurtosis-0.596
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha5259000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.927; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1s51a_
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
Domain ID domain_idd1s51b_
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 (2 domains)

Domain ID domain_id1s51A00
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
Domain ID domain_id1s51B00
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)