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Solution structure of the N-terminal soluble domains of bacillus subtilis copa

Analyse Solution structure of the N-terminal soluble domains of bacillus subtilis copa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2RML
Type: protein
Length: 147 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Copper-transporting P-type ATPase copa
EC: 3.6.3.-
UniProt: O32220
Pockets: 1 · best druggability 0.47

Structure

solution nmr · 1 distinct chain · 27% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Copper-transporting P-type ATPase copa (EC 3.6.3.-)	protein	147	27% helix, 29% strand	O32220

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	79	0.47	0.82	25	empty

Compared structures

2RML · Solution structure of the N-terminal soluble domains of Bacillus subtilis CopA · the same entry in another collection · chain A against A, TM-score 1.00
O32220 · AlphaFold monomer V2.0 prediction for copper-exporting P-type ATPase (O32220) · a predicted model of the same protein · chain A against A, TM-score 0.65

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 O32220
Elsewhere: RCSB PDB 2RML · PDBe 2RML · UniProt O32220

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