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Ec-NMR structure of ralstonia metallidurans RMET_5065 determined by combining evolutionary couplings (ec) and sparse NMR data. northeast structural genomics consortium target CRR115

Analyse Ec-NMR structure of ralstonia metallidurans RMET_5065 determined by combining… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2N4B
Type: protein
Length: 138 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
UniProt: Q1LD49
Pockets: 1 · best druggability 0.75

Structure

solution nmr · 1 distinct chain · 27% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein	protein	138	27% helix, 36% strand	Q1LD49

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	354	0.75	0.85	34	empty

Compared structures

2N4B · EC-NMR Structure of Ralstonia metallidurans Rmet_5065 Determined by Combining… · 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
Every structure of UniProt Q1LD49
Elsewhere: RCSB PDB 2N4B · PDBe 2N4B · UniProt Q1LD49

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