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Tcdb and frizzled-2 crd complex

Analyse Tcdb and frizzled-2 crd complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7N9S
Type: protein
Length: 2,486 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Frizzled-2; Toxin B
EC: 3.4.22.-
UniProt: Q14332, P18177
Pockets: 20 · best druggability 0.57

Structure

electron microscopy · 2 distinct chains · 0% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Frizzled-2	protein	121	0% helix, 0% strand	Q14332
A	Toxin B (EC 3.4.22.-)	protein	2365	0% helix, 0% strand	P18177

Pockets

20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	456	0.57	0.73	87	empty
2	403	0.57	0.74	68	empty
3	479	0.55	0.72	95	empty
4	410	0.55	0.73	57	empty
5	358	0.53	0.73	65	empty

Interfaces

1 interface between chains.

B–A · 51 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

7N9S · TcdB and frizzled-2 CRD complex · the same entry in another collection · chain B against B, TM-score 1.00
Q14332 · AlphaFold monomer V2.0 prediction for frizzled-2 (Q14332) · a predicted model of the same protein · chain B against A, TM-score 0.95

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 Q14332
Every structure of UniProt P18177
Elsewhere: RCSB PDB 7N9S · PDBe 7N9S · UniProt Q14332 · UniProt P18177

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