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Crystal structure of ABC sugar transporter subunit from rhodobacter sphaeroides 2.4.1

Analyse Crystal structure of ABC sugar transporter subunit from rhodobacter sphaeroides… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3L49
Type
protein
Length
1,128 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ABC sugar (ribose) transporter, periplasmic substrate- binding subunit
UniProt
Q3J3W0
Ligands
UNL
Pockets
15 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DABC sugar (ribose) transporter, periplasmic substrate- binding subunitprotein28245% helix, 21% strandQ3J3W0

Ligands and binding sites

  • UNL · Unknown ligand · ligand · 4 copies · chains A, B, C, D

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

Pockets

15 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17660.780.8279UNL
27080.770.8285empty
3750.740.9718UNL
4610.720.9818UNL
53720.720.8345empty

Interfaces

5 interfaces between chains.

  • A–B · 1000 Ų buried · 6 hydrogen bonds · protein-protein
  • C–D · 997 Ų buried · 7 hydrogen bonds · protein-protein
  • B–D · 413 Ų buried · 7 hydrogen bonds · protein-protein
  • A–C · 257 Ų buried · 2 hydrogen bonds · protein-protein
  • B–C · 122 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 3L49 · CRYSTAL STRUCTURE OF ABC SUGAR TRANSPORTER SUBUNIT FROM Rhodobacter sphaeroides 2.4.1 · the same entry in another collection · chain A against A, TM-score 1.00

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