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Solution NMR structure of the apo-nosl protein from achromobacter cycloclastes

Analyse Solution NMR structure of the apo-nosl protein from achromobacter cycloclastes in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2HPU
Type: protein
Length: 126 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nosl protein
UniProt: O68481
Pockets: 1 · best druggability 0.32

Structure

solution nmr · 1 distinct chain · 25% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nosl protein	protein	126	25% helix, 28% strand	O68481

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	62	0.32	0.76	19	empty

Compared structures

2HPU · Solution NMR structure of the apo-NosL protein from Achromobacter cycloclastes · the same entry in another collection · chain A against A, TM-score 1.00
O68481 · AlphaFold monomer V2.0 prediction for copper-binding lipoprotein nosl (O68481) · a predicted model of the same protein · chain A against A, TM-score 0.60

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 O68481
Elsewhere: RCSB PDB 2HPU · PDBe 2HPU · UniProt O68481

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