4xes

Structure of active-like neurotensin receptor

Method: X-RAY DIFFRACTION Dmax: 101.9 Å Quality: GOOD

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

Neurotensin receptor type 1, Endolysin chimera

Enterobacteria phage T4

UniProt P00720

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–161 Fragment:UNP residues 43-396 (P20789), residues 2-161 (P00720) Mutation:A86L, E166A, G215A, V360A Neurotensin/neuromedin N × 1 (P20068) CIT CITRIC ACID × 1 PEG DI(HYDROXYETHYL)ETHER × 5 GOL GLYCEROL × 3 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;293 K;19.8-23.4% PEG400, 80 mM HEPES, 50 mM lithium citrate, 2 mM TCEP Resolution 2.60 Å R-free 0.280

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.

721 other PDB entries and 846 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ENLYS_BPT4
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 378–537; UniProt 2–161

Neurotensin receptor type 1, Endolysin chimera

Enterobacteria phage T4

UniProt P20789

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 43–396 Fragment:UNP residues 43-396 (P20789), residues 2-161 (P00720) Mutation:A86L, E166A, G215A, V360A Neurotensin/neuromedin N × 1 (P20068) CIT CITRIC ACID × 1 PEG DI(HYDROXYETHYL)ETHER × 5 GOL GLYCEROL × 3 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;293 K;19.8-23.4% PEG400, 80 mM HEPES, 50 mM lithium citrate, 2 mM TCEP Resolution 2.60 Å R-free 0.280

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.

24 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NTR1_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 11–364; UniProt 43–396

Neurotensin/neuromedin N

OrganismNot specified

UniProt P20068

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 157–162 Fragment:UNP residues 157-162 Neurotensin receptor type 1, Endolysin chimera × 1 (P20789,P00720) CIT CITRIC ACID × 1 PEG DI(HYDROXYETHYL)ETHER × 5 GOL GLYCEROL × 3 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;293 K;19.8-23.4% PEG400, 80 mM HEPES, 50 mM lithium citrate, 2 mM TCEP Resolution 2.60 Å R-free 0.280

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.

12 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NEUT_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–6; UniProt 157–162

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 4xes

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4xes
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4xes
Deposition date deposition_date2014-12-24
Structure title titleStructure of active-like neurotensin receptor
Keywords keywordsmembrane protein, G protein-coupled receptor, GPCR, neurotensin receptor, NTSR1, SIGNALING PROTEIN, HYDROLASE; SIGNALING PROTEIN, HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.41
Radius of gyration Rg (electron density) rg_electron29.68
Forward intensity I(0) i044785500.00
Molecular weight molecular_weight54972.0 kDa
Excluded volume excluded_volume70027 ų
Envelope volume envelope_volume86664 ų
Hydration-shell volume shell_volume26369 ų
Envelope diameter envelope_diameter105.9
Shell Rg shell_rg34.21
Envelope Rg envelope_rg29.62
Shape Rg shape_rg29.69
Total Rg total_rg30.12
Total atoms total_atoms3868
Residues n_residues477
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 dmax101.9
Rg (real space) rg_real30.70
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real4.4790e+07
I(0) uncertainty (real space) i0_real_error7.2580e+05
Rg (reciprocal space) rg_reciprocal30.58
I(0) (reciprocal space) i0_reciprocal44780000.0000
Solution quality estimate total_estimate0.8195
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary25.5
Skewness Skewness skewness0.485
Kurtosis Kurtosis kurtosis-0.529
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha11390000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.738; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.610; Smooth: 0.827

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4xesA01
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_id4xesA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily40

8. Citations (1)

9. Files and Curves (10)