MolNFT v1 · #185267 · protein

HSPEPT2 bound to ala-phe in the inward facing partially occluded conformation

7PMY · Solute carrier family 15 member 2: “HSPEPT2 bound to ala-phe in the inward facing partially occluded conformation”. Electron microscopy, 7 pockets (best druggability 0.76). MolNFT v1 #185267 on GenesisL1: 3D structure, binding sites…

PDB: 7PMY
Type: protein
Length: 659 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Solute carrier family 15 member 2; Ala-phe
UniProt: Q16348
Pockets: 7 · best druggability 0.76

Structure

electron microscopy · 2 distinct chains · 56% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Solute carrier family 15 member 2	protein	657	56% helix, 18% strand	Q16348
B	Ala-phe	protein	2	0% helix, 0% strand	—

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	83	0.76	0.99	22	empty
2	366	0.76	0.86	41	empty
3	671	0.75	0.81	74	empty
4	219	0.52	0.76	20	empty
5	170	0.48	0.76	26	empty

Interfaces

1 interface between chains.

A–B · 297 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

7PMY · HsPepT2 bound to Ala-Phe in the inward facing partially occluded conformation · the same entry in another collection · chain A against A, TM-score 1.00
Q16348 · AlphaFold monomer V2.0 prediction for solute carrier family 15 member 2 (Q16348) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 Q16348
Elsewhere: RCSB PDB 7PMY · PDBe 7PMY · UniProt Q16348

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