Research workbench

Membrane protein at 2.8 ångströms

Analyse Membrane protein at 2.8 ångströms in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5DIR
Type: protein
Length: 620 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9HVM5

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	157	—	Q9HVM5
B	—	protein	149	—	Q9HVM5
C, D	—	protein	149	—	Q9HVM5
E, F, G, H	—	protein	4	—	—

Compared structures

5DIR · membrane protein at 2.8 Angstroms · the same entry in another collection · chain H against H, TM-score 1.00
Q9HVM5 · AlphaFold monomer V2.0 prediction for lipoprotein signal peptidase (Q9HVM5) · a predicted model of the same protein · chain C against A, TM-score 0.96

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 Q9HVM5
Elsewhere: RCSB PDB 5DIR · PDBe 5DIR · UniProt Q9HVM5

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