3coc

Crystal Structure of D115A mutant of Bacteriorhodopsin

Method: X-RAY DIFFRACTION Dmax: 80.0 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 14–262 Mutation:D128A RET RETINAL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.5;310 K;1.4 M NaH2PO4 (pH 3.7), 0.8 M NaH2PO4 (pH 4.5), and 0.12 M hexanediol, bicelle method, temperature 310K Resolution 2.31 Å R-free 0.275
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 14–262 Mutation:D128A RET RETINAL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.5;310 K;1.4 M NaH2PO4 (pH 3.7), 0.8 M NaH2PO4 (pH 4.5), and 0.12 M hexanediol, bicelle method, temperature 310K Resolution 2.31 Å R-free 0.275

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_HALSA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–249; UniProt 14–262 Author chain B; PDBConstruct 1–249; UniProt 14–262

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 3coc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3coc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3coc
Deposition date deposition_date2008-03-27
Structure title titleCrystal Structure of D115A mutant of Bacteriorhodopsin
Keywords keywords;membrane protein, membrane protein folding, hydrogen bond, Chromophore, Hydrogen ion transport, Ion transport, Photoreceptor protein, Pyrrolidone carboxylic acid, Receptor, Retinal protein, Sensory transduction, Transmembrane, Transport, 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_guinier25.16
Radius of gyration Rg (electron density) rg_electron24.03
Forward intensity I(0) i031227800.00
Molecular weight molecular_weight50112.0 kDa
Excluded volume excluded_volume65649 ų
Envelope volume envelope_volume74289 ų
Hydration-shell volume shell_volume25763 ų
Envelope diameter envelope_diameter81.3
Shell Rg shell_rg31.14
Envelope Rg envelope_rg24.04
Shape Rg shape_rg24.04
Total Rg total_rg24.94
Total atoms total_atoms3546
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 dmax80.0
Rg (real space) rg_real25.08
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real3.1230e+07
I(0) uncertainty (real space) i0_real_error3.8650e+05
Rg (reciprocal space) rg_reciprocal25.11
I(0) (reciprocal space) i0_reciprocal31230000.0000
Solution quality estimate total_estimate0.9091
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.2
Skewness Skewness skewness0.162
Kurtosis Kurtosis kurtosis-0.603
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4883000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.944; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.995

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_idd3coca_
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_idd3cocb_
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_id3cocA00
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_id3cocB00
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)