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Dimeric apoa-IV

Analyse Dimeric apoa-IV in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3S84
Type: protein
Length: 480 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Apolipoprotein a-IV
UniProt: P06727
Ligands: SO4
Pockets: 3 · best druggability 0.60

Structure

x-ray diffraction · 2 distinct chains · 92% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Apolipoprotein a-IV	protein	239	93% helix, 0% strand	P06727
B	Apolipoprotein a-IV	protein	241	91% helix, 0% strand	P06727

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains B

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

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	187	0.60	0.82	28	empty
2	114	0.43	0.77	14	empty
3	76	0.38	0.77	11	empty

Interfaces

1 interface between chains.

A–B · 6358 Å² buried · 57 hydrogen bonds · protein-protein

Compared structures

3S84 · Dimeric apoA-IV · the same entry in another collection · chain A against A, TM-score 1.00
P06727 · AlphaFold monomer V2.0 prediction for apolipoprotein a-IV (P06727) · a predicted model of the same protein · chain A against A, TM-score 0.88

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 P06727
Elsewhere: RCSB PDB 3S84 · PDBe 3S84 · UniProt P06727

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