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Lactobacillus casei HPRK/P bound to phosphate

Analyse Lactobacillus casei HPRK/P bound to phosphate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1JB1
Type: protein
Length: 161 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hprk protein
EC: 2.7.1.-, 3.1.3.-
UniProt: Q9RE09
Ligands: PO4

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hprk protein (EC 2.7.1.-, 3.1.3.-)	protein	161	31% helix, 31% strand	Q9RE09

Ligands and binding sites

PO4 · Phosphate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

1JB1 · Lactobacillus casei HprK/P Bound to Phosphate · the same entry in another collection · chain A against A, TM-score 1.00
Q9RE09 · AlphaFold monomer V2.0 prediction for hpr KINASE/PHOSPHORYLASE (Q9RE09) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 Q9RE09
Elsewhere: RCSB PDB 1JB1 · PDBe 1JB1 · UniProt Q9RE09

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