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Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins

Analyse Structure and dynamics conspire in the evolution of affinity between… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6ES5
Type: protein
Length: 95 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cid; Ncbd
Pockets: 1 · best druggability 0.57

Structure

solution nmr · 2 distinct chains · 63% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cid	protein	45	53% helix, 0% strand	—
B	Ncbd	protein	50	72% helix, 0% strand	—

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	194	0.57	0.80	32	empty

Interfaces

1 interface between chains.

A–B · 940 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

6ES5 · Structure and dynamics conspire in the evolution of affinity between intrinsically… · 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
Elsewhere: RCSB PDB 6ES5 · PDBe 6ES5

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