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Arginase from medicago truncatula

Analyse Arginase from medicago truncatula in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6VSS
Type
protein
Length
1,905 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Arginase
EC
3.5.3.1
UniProt
G7JFU5
Ligands
MN
Pockets
17 · best druggability 0.88

Structure

x-ray diffraction · 4 distinct chains · 45% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AArginase (EC 3.5.3.1)protein31646% helix, 18% strandG7JFU5
BArginase (EC 3.5.3.1)protein31945% helix, 18% strandG7JFU5
C, D, FArginase (EC 3.5.3.1)protein31845% helix, 18% strandG7JFU5
EArginase (EC 3.5.3.1)protein31645% helix, 18% strandG7JFU5

Ligands and binding sites

  • MN · Manganese (II) ion · metal · 12 copies · chains A, B, C, D, E, F

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

Pockets

17 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18360.880.91112empty
23670.820.9148empty
38210.800.8380empty
48080.790.8277empty
55270.730.8258empty

Interfaces

12 interfaces between chains.

  • B–E · 1756 Ų buried · 27 hydrogen bonds · protein-protein
  • A–D · 1717 Ų buried · 21 hydrogen bonds · protein-protein
  • C–F · 1686 Ų buried · 20 hydrogen bonds · protein-protein
  • A–B · 924 Ų buried · 9 hydrogen bonds · protein-protein
  • B–C · 897 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 6VSS · Arginase from Medicago truncatula · the same entry in another collection · chain F against F, TM-score 1.00
  • G7JFU5 · AlphaFold monomer V2.0 prediction for arginase, mitochondrial (G7JFU5) · a predicted model of the same protein · chain D against A, TM-score 1.00

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