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Cryo-EM structure of TMEM87A

Analyse Cryo-EM structure of TMEM87A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8CTJ
Type: protein
Length: 401 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transmembrane protein 87A
UniProt: Q8NBN3
Ligands: PEE
Pockets: 5 · best druggability 0.81

Structure

electron microscopy · 1 distinct chain · 55% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transmembrane protein 87A	protein	401	55% helix, 14% strand	Q8NBN3

Ligands and binding sites

PEE · 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine · ligand · chains A

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1077	0.81	0.82	86	PEE
2	242	0.71	0.86	36	empty
3	118	0.43	0.77	15	empty
4	97	0.34	0.74	14	empty
5	65	0.34	0.76	14	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

8CTJ · Cryo-EM structure of TMEM87A · the same entry in another collection · chain A against A, TM-score 1.00
Q8NBN3 · AlphaFold monomer V2.0 prediction for transmembrane protein 87A (Q8NBN3) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 Q8NBN3
Elsewhere: RCSB PDB 8CTJ · PDBe 8CTJ · UniProt Q8NBN3

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