Research workbench

PSF4 in complex with MN2+ and (R)-2-hpp

Analyse PSF4 in complex with MN2+ and (R)-2-hpp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5U5D
Type: protein
Length: 741 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9JN69
Ligands: TB6, MN

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	—	protein	187	—	Q9JN69
D	—	protein	180	—	Q9JN69

Ligands and binding sites

TB6 · [(2R)-2-hydroxypropyl]phosphonic acid · ligand · 3 copies · chains A, C, B, D
MN · Manganese (II) ion · metal · 3 copies · chains A, B, D

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

Compared structures

5U5D · Psf4 in complex with Mn2+ and (R)-2-HPP · the same entry in another collection · chain A against A, TM-score 1.00
Q9JN69 · AlphaFold monomer V2.0 prediction for (S)-2-hydroxypropylphosphonic acid epoxidase… · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q9JN69
Elsewhere: RCSB PDB 5U5D · PDBe 5U5D · UniProt Q9JN69

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