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Crystal structure of catalytic domain of human phospholipase D1

Analyse Crystal structure of catalytic domain of human phospholipase D1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6U8Z
Type: protein
Length: 568 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q13393
Ligands: PO3

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	568	—	Q13393

Ligands and binding sites

PO3 · Phosphite ion · ion · chains A

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

Compared structures

6U8Z · Crystal Structure of Catalytic Domain of Human Phospholipase D1 · the same entry in another collection · chain A against A, TM-score 1.00
Q13393 · AlphaFold monomer V2.0 prediction for phospholipase D1 (Q13393) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q13393
Elsewhere: RCSB PDB 6U8Z · PDBe 6U8Z · UniProt Q13393

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