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Structure of human phospholipase D2 catalytic domain

Analyse Structure of human phospholipase D2 catalytic domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6OHO
Type: protein
Length: 1,159 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: O14939
Ligands: SO4

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	580	—	O14939
B	—	protein	579	—	O14939

Ligands and binding sites

SO4 · Sulfate ion · ion · 17 copies · chains A, B
GOL · Glycerol · additive · 8 copies · chains A, B
DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · chains B

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

Compared structures

6OHO · Structure of human Phospholipase D2 catalytic domain · the same entry in another collection · chain A against A, TM-score 1.00
O14939 · AlphaFold monomer V2.0 prediction for phospholipase D2 (O14939) · a predicted model of the same protein · chain B against A, TM-score 1.00

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 O14939
Elsewhere: RCSB PDB 6OHO · PDBe 6OHO · UniProt O14939

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