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Crystal structure of putative isomerase from sinorhizobium meliloti

Analyse Crystal structure of putative isomerase from sinorhizobium meliloti in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2PPG
Type
protein
Length
1,522 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative isomerase
UniProt
Q92ZS5
Pockets
18 · best druggability 0.86

Structure

x-ray diffraction · 4 distinct chains · 41% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative isomeraseprotein38742% helix, 22% strandQ92ZS5
BPutative isomeraseprotein37042% helix, 24% strandQ92ZS5
CPutative isomeraseprotein38240% helix, 22% strandQ92ZS5
DPutative isomeraseprotein38339% helix, 21% strandQ92ZS5

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19930.860.88107empty
23830.860.9441empty
33840.850.9441empty
45940.780.8463empty
52710.740.8849empty

Interfaces

5 interfaces between chains.

  • A–C · 2294 Ų buried · 33 hydrogen bonds · protein-protein
  • B–C · 1072 Ų buried · 20 hydrogen bonds · protein-protein
  • A–D · 1060 Ų buried · 20 hydrogen bonds · protein-protein
  • C–D · 476 Ų buried · 6 hydrogen bonds · protein-protein
  • A–B · 459 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 36 modified (engineered).

Compared structures

  • 2PPG · Crystal structure of putative isomerase from Sinorhizobium meliloti · the same entry in another collection · chain A against A, TM-score 1.00

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