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Manipulating the coupled folding and binding process drives affinity maturation in a protein-protein complex

Analyse Manipulating the coupled folding and binding process drives affinity maturation… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3BVG
Type: protein
Length: 228 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Enterotoxin type C-3
UniProt: P0A0L5
Ligands: ZN
Pockets: 2 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Enterotoxin type C-3	protein	228	21% helix, 36% strand	P0A0L5

Ligands and binding sites

ZN · Zinc ion · metal · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	69	0.37	0.78	16	empty
2	61	0.30	0.74	15	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

3BVG · Manipulating the coupled folding and binding process drives affinity maturation in a… · the same entry in another collection · chain A against A, TM-score 1.00
P0A0L5 · AlphaFold monomer V2.0 prediction for enterotoxin type C-3 (P0A0L5) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P0A0L5
Elsewhere: RCSB PDB 3BVG · PDBe 3BVG · UniProt P0A0L5

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