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Crystal structure of geodermatophilus obscurus L-ribose isomerase

Analyse Crystal structure of geodermatophilus obscurus L-ribose isomerase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5AVP
Type
protein
Length
960 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
L-ribose isomerase
EC
5.3.1.-
UniProt
D2S5K0
Ligands
MN
Pockets
15 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DL-ribose isomerase (EC 5.3.1.-)protein24021% helix, 31% strandD2S5K0

Ligands and binding sites

  • MN · Manganese (II) ion · metal · 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
11520.680.8822empty
21170.660.8921empty
32400.630.8237MN
44340.620.7743empty
54120.610.7638empty

Interfaces

6 interfaces between chains.

  • A–B · 2418 Ų buried · 33 hydrogen bonds · protein-protein
  • C–D · 2354 Ų buried · 36 hydrogen bonds · protein-protein
  • A–D · 936 Ų buried · 16 hydrogen bonds · protein-protein
  • B–C · 924 Ų buried · 12 hydrogen bonds · protein-protein
  • B–D · 112 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 5AVP · Crystal structure of Geodermatophilus obscurus L-ribose isomerase · the same entry in another collection · chain A against A, TM-score 1.00

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