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Outward facing conformation of the metni methionine ABC transporter in complex with lipo-metq

Analyse Outward facing conformation of the metni methionine ABC transporter in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7MBZ
Type
protein
Length
1,172 residues
Chains
5
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ABC transporter, permease protein; Lipoprotein; ABC transporter, ATP-binding protein
UniProt
Q9JXP3, Q7DD63, Q9JXP2
Pockets
16 · best druggability 0.87

Structure

electron microscopy · 4 distinct chains · 48% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BABC transporter, permease proteinprotein22284% helix, 0% strandQ9JXP3
ELipoproteinprotein24138% helix, 22% strandQ7DD63
CABC transporter, ATP-binding proteinprotein24238% helix, 19% strandQ9JXP2
DABC transporter, ATP-binding proteinprotein24534% helix, 20% strandQ9JXP2

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110090.870.88133empty
211620.850.85140empty
39410.830.85129empty
41590.770.9335empty
56770.770.8294empty

Interfaces

6 interfaces between chains.

  • A–B · 1702 Ų buried · 10 hydrogen bonds · protein-protein
  • C–D · 1306 Ų buried · 21 hydrogen bonds · protein-protein
  • E–B · 953 Ų buried · 14 hydrogen bonds · protein-protein
  • B–D · 862 Ų buried · 7 hydrogen bonds · protein-protein
  • A–C · 826 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 7MBZ · Outward facing conformation of the MetNI methionine ABC transporter in complex with… · the same entry in another collection · chain A against A, TM-score 1.00

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