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MBP-L30

Analyse MBP-L30 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1NMU
Type
protein
Length
943 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Maltose-binding periplasmic protein; 60S ribosomal protein L30
UniProt
P02928, P14120
Ligands
GLC
Pockets
11 · best druggability 0.74

Structure

x-ray diffraction · 3 distinct chains · 44% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CMaltose-binding periplasmic proteinprotein36845% helix, 21% strandP02928
B60S ribosomal protein L30protein10446% helix, 18% strandP14120
D60S ribosomal protein L30protein10340% helix, 17% strandP14120

Ligands and binding sites

  • GLC · alpha-D-glucopyranose · sugar · 8 copies · chains A, C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110970.740.7787empty
27410.740.7955GLC
33680.720.8431GLC
42430.500.7534empty
51190.460.7937empty

Interfaces

4 interfaces between chains.

  • B–C · 741 Ų buried · 7 hydrogen bonds · protein-protein
  • A–B · 371 Ų buried · 7 hydrogen bonds · protein-protein
  • A–C · 339 Ų buried · 7 hydrogen bonds · protein-protein
  • C–D · 298 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 1NMU · MBP-L30 · the same entry in another collection · chain A against A, TM-score 1.00
  • P14120 · AlphaFold monomer V2.0 prediction for 60S ribosomal protein L30 (P14120) · a predicted model of the same protein · chain D against A, TM-score 0.93

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