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NMR structure of monomeric car D1 domain

Analyse NMR structure of monomeric car D1 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1RSF
Type: protein
Length: 126 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Coxsackievirus and adenovirus receptor
UniProt: P78310
Pockets: 1 · best druggability 0.41

Structure

solution nmr · 1 distinct chain · 5% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Coxsackievirus and adenovirus receptor	protein	126	5% helix, 45% strand	P78310

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	54	0.41	0.82	17	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1RSF · NMR Structure of Monomeric CAR d1 domain · the same entry in another collection · chain A against A, TM-score 1.00
P78310 · AlphaFold monomer V2.0 prediction for coxsackievirus and adenovirus receptor (P78310) · a predicted model of the same protein · chain A against A, TM-score 0.85

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 P78310
Elsewhere: RCSB PDB 1RSF · PDBe 1RSF · UniProt P78310

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