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Cryo-EM structure of dolphin prestin: inhibited I (chloride + salicylate)

Analyse Cryo-EM structure of dolphin prestin: inhibited I (chloride + salicylate) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7S9A
Type: protein
Length: 1,350 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Prestin
UniProt: D7PC76
Ligands: SAL
Pockets: 20 · best druggability 0.84

Structure

electron microscopy · 1 distinct chain · 57% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Prestin	protein	675	57% helix, 5% strand	D7PC76

Ligands and binding sites

SAL · 2-hydroxybenzoic acid · ligand · 2 copies · chains A, B

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

Pockets

20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1002	0.84	0.85	75	empty
2	335	0.75	0.86	37	empty
3	346	0.73	0.85	39	empty
4	420	0.71	0.82	43	SAL
5	397	0.71	0.82	44	SAL

Interfaces

1 interface between chains.

A–B · 3649 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

7S9A · Cryo-EM Structure of dolphin Prestin: Inhibited I (Chloride + Salicylate) · the same entry in another collection · chain A against A, TM-score 1.00

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 D7PC76
Elsewhere: RCSB PDB 7S9A · PDBe 7S9A · UniProt D7PC76

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