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Backbone and side chain 1H, 13C, and 15N chemical shift assignments for edb and specific binding aptide

Analyse Backbone and side chain 1H, 13C, and 15N chemical shift assignments for edb and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2MNU
Type: protein
Length: 119 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Edb; Apt
Pockets: 1 · best druggability 0.74

Structure

solution nmr · 2 distinct chains · 0% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Edb	protein	93	0% helix, 33% strand	—
B	Apt	protein	26	0% helix, 27% 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	319	0.74	0.86	51	empty

Interfaces

1 interface between chains.

A–B · 739 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

2MNU · Backbone and side chain 1H, 13C, and 15N Chemical Shift Assignments for EDB and specific… · 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 2MNU · PDBe 2MNU

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