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Crystal structure of pseudomonas stutzeri L-rhamnose isomerase mutant S329L in complex with L-rhamnose

Analyse Crystal structure of pseudomonas stutzeri L-rhamnose isomerase mutant S329L in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3M0V
Type
protein
Length
1,704 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
L-rhamnose isomerase
EC
5.3.1.14
UniProt
Q75WH8
Ligands
RNS, MN
Pockets
20 · best druggability 0.88

Structure

x-ray diffraction · 3 distinct chains · 49% helix, 11% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BL-rhamnose isomerase (EC 5.3.1.14)protein42149% helix, 10% strandQ75WH8
CL-rhamnose isomerase (EC 5.3.1.14)protein43348% helix, 10% strandQ75WH8
DL-rhamnose isomerase (EC 5.3.1.14)protein42949% helix, 11% strandQ75WH8

Ligands and binding sites

  • RNS · L-rhamnose · ligand · 4 copies · chains A, B, C, D
  • MN · Manganese (II) ion · metal · 8 copies · chains A, B, C, D

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14550.880.9599empty
210210.830.84104empty
39490.820.8390empty
41350.810.9829empty
51420.800.9730empty

Interfaces

6 interfaces between chains.

  • C–D · 2727 Ų buried · 24 hydrogen bonds · protein-protein
  • B–D · 2441 Ų buried · 23 hydrogen bonds · protein-protein
  • A–C · 2411 Ų buried · 26 hydrogen bonds · protein-protein
  • A–B · 1980 Ų buried · 16 hydrogen bonds · protein-protein
  • B–C · 1711 Ų buried · 19 hydrogen bonds · protein-protein

Compared structures

  • 3M0V · Crystal structure of Pseudomonas stutzeri L-rhamnose isomerase mutant S329L in complex… · the same entry in another collection · chain A against A, TM-score 1.00

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