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Cryo-EM of aedes aegypti TOLL5A

Analyse Cryo-EM of aedes aegypti TOLL5A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7B1D
Type: protein
Length: 1,505 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Toll-like receptor
UniProt: A0A6I8TEX2
Ligands: NAG
Pockets: 13 · best druggability 0.81

Structure

electron microscopy · 2 distinct chains · 8% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Toll-like receptor	protein	753	8% helix, 19% strand	A0A6I8TEX2
C	Toll-like receptor	protein	752	7% helix, 16% strand	A0A6I8TEX2

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 12 copies · chains B, C

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

Pockets

13 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1069	0.81	0.83	103	empty
2	681	0.81	0.85	85	empty
3	212	0.66	0.84	31	empty
4	117	0.64	0.87	25	empty
5	412	0.62	0.77	46	empty

Interfaces

1 interface between chains.

B–C · 1096 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 disulfide, 8 glycan (disulfide, N-glycosylation).

Compared structures

7B1D · Cryo-EM of Aedes Aegypti Toll5A · the same entry in another collection · chain B against B, 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 A0A6I8TEX2
Elsewhere: RCSB PDB 7B1D · PDBe 7B1D · UniProt A0A6I8TEX2

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