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Crystal structure of human dehydrodolichyl diphosphate synthase (NGBR/DHDDS) in complex with mg and ipp

Analyse Crystal structure of human dehydrodolichyl diphosphate synthase (NGBR/DHDDS) in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6W2L
Type: protein
Length: 523 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q86SQ9, Q96E22
Ligands: IPE, MG

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	328	—	Q86SQ9
B	—	protein	195	—	Q96E22

Ligands and binding sites

IPE · 3-methylbut-3-enyl trihydrogen diphosphate · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · chains A, B

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

Compared structures

6W2L · Crystal structure of human dehydrodolichyl diphosphate synthase (NgBR/DHDDS) in complex… · the same entry in another collection · chain A against A, TM-score 1.00
Q86SQ9 · AlphaFold monomer V2.0 prediction for dehydrodolichyl diphosphate synthase complex… · a predicted model of the same protein · chain A against A, TM-score 0.99
Q96E22 · AlphaFold monomer V2.0 prediction for dehydrodolichyl diphosphate synthase complex… · a predicted model of the same protein · chain B 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 Q86SQ9
Every structure of UniProt Q96E22
Elsewhere: RCSB PDB 6W2L · PDBe 6W2L · UniProt Q86SQ9 · UniProt Q96E22

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