Research workbench

HSPEPT1 bound to ala-phe in the outward facing open conformation

Analyse HSPEPT1 bound to ala-phe in the outward facing open conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7PMX
Type: protein
Length: 659 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Solute carrier family 15 member 1; Ala-phe
UniProt: P46059
Pockets: 9 · best druggability 0.74

Structure

electron microscopy · 2 distinct chains · 54% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Solute carrier family 15 member 1	protein	657	54% helix, 14% strand	P46059
B	Ala-phe	protein	2	0% helix, 0% strand	—

Pockets

9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	105	0.74	0.94	26	empty
2	702	0.73	0.79	44	empty
3	343	0.61	0.78	47	empty
4	196	0.57	0.80	28	empty
5	186	0.52	0.77	23	empty

Interfaces

1 interface between chains.

A–B · 298 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

7PMX · HsPepT1 bound to Ala-Phe in the outward facing open conformation · the same entry in another collection · chain A against A, TM-score 1.00
P46059 · AlphaFold monomer V2.0 prediction for solute carrier family 15 member 1 (P46059) · a predicted model of the same protein · chain A against A, TM-score 0.87

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 P46059
Elsewhere: RCSB PDB 7PMX · PDBe 7PMX · UniProt P46059

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