2ksb

Substance P in isotropic q=0.25 DMPC/CHAPS/GM1 bicelles as a ligand for NK1R

Method: SOLUTION NMR
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Substance-P receptor

OrganismNot specified

UniProt P25103

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 2 Substance P × 1 (P20366) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name NK1R_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–364; UniProt 1–364

Substance P

OrganismNot specified

UniProt P20366

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 2 Substance-P receptor × 1 (P25103) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name TKN1_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–11; UniProt 58–68

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id2ksb
Deposition date deposition_date2009-12-31
Structure title titleSubstance P in isotropic q=0.25 DMPC/CHAPS/GM1 bicelles as a ligand for NK1R
Keywords keywordsSubstance P, DMPC/CHAPS/GM1 bicelle, Autodock, NK1R, NEUROPEPTIDE RECEPTOR-NEUROPEPTIDE complex; NEUROPEPTIDE RECEPTOR/NEUROPEPTIDE
Experimental Method methodSOLUTION NMR
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

2ksb__assembly_1__model_2

Assembly 1 · Model 2 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2ksb__assembly_1__model_2 | I(q)

10-2 10-1 105 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

2ksb__assembly_1__model_2 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)24.54 Å
Rg (electron density)23.60 Å
Total Rg24.47 Å
Atom count6061
Residues374
Excluded volume55035 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 2ksb__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 2 2ksb__assembly_1__model_2 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 3 2ksb__assembly_1__model_3 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 4 2ksb__assembly_1__model_4 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 5 2ksb__assembly_1__model_5 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (2)

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6. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2ksbA00
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
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7. Citations (1)