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Structure of constitutively active neurotensin receptor

Analyse Structure of constitutively active neurotensin receptor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5T04
Type: protein
Length: 464 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Neurotensin receptor type 1,ENDOLYSIN,NEUROTENSIN receptor type 1; Arg-arg-pro-tyr-ile-leu
EC: 3.2.1.17
UniProt: P20789, P00720
Ligands: TCE
Pockets: 3 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 70% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Neurotensin receptor type 1,ENDOLYSIN,NEUROTENSIN receptor type 1 (EC 3.2.1.17)	protein	458	71% helix, 5% strand	P20789, P00720
B	Arg-arg-pro-tyr-ile-leu	protein	6	0% helix, 0% strand	—

Ligands and binding sites

TCE · 3,3',3''-phosphanetriyltripropanoic acid · ligand · chains A
PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A
GOL · Glycerol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	322	0.57	0.75	44	empty
2	172	0.43	0.74	28	empty
3	69	0.39	0.78	13	empty

Interfaces

1 interface between chains.

A–B · 858 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5T04 · Structure of constitutively active neurotensin receptor · the same entry in another collection · chain A against A, TM-score 1.00
P20789 · AlphaFold monomer V2.0 prediction for neurotensin receptor type 1 (P20789) · a predicted model of the same protein · chain A against A, TM-score 0.64

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P20789
Every structure of UniProt P00720
Elsewhere: RCSB PDB 5T04 · PDBe 5T04 · UniProt P20789 · UniProt P00720

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