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Ovine (B0,+AT-RBAT)2 hetero-tetramer, asymmetric unit, rigid-body fitted

Analyse Ovine (B0,+AT-RBAT)2 hetero-tetramer, asymmetric unit, rigid-body fitted in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7NF8
Type
protein
Length
1,078 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
B(0,+)-type amino acid transporter 1; Neutral and basic amino acid transport protein rbat
UniProt
A0A6P3EL78, A0A6P7DVK7
Ligands
CLR, LBN, NAG, CA
Pockets
10 · best druggability 0.75

Structure

electron microscopy · 2 distinct chains · 47% helix, 11% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
BB(0,+)-type amino acid transporter 1protein45573% helix, 1% strandA0A6P3EL78
ANeutral and basic amino acid transport protein rbatprotein62328% helix, 19% strandA0A6P7DVK7

Ligands and binding sites

  • CLR · Cholesterol · ligand · 2 copies · chains B, A
  • LBN · 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine · ligand · chains B, A
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A
  • CA · Calcium ion · metal · chains A

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

Pockets

10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16480.750.8166empty
23460.740.8548empty
37870.730.7980empty
45670.680.7760empty
51500.470.7724empty

Interfaces

1 interface between chains.

  • B–A · 1614 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 glycan, 4 disulfide (N-glycosylation, disulfide).

Compared structures

  • 7NF8 · Ovine (b0,+AT-rBAT)2 hetero-tetramer, asymmetric unit, rigid-body fitted · the same entry in another collection · chain B against B, TM-score 1.00

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