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Altering the binuclear manganese cluster of arginase diminishes thermostability and catalytic function

Analyse Altering the binuclear manganese cluster of arginase diminishes thermostability… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4RLA
Type
protein
Length
942 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.94
Source
Rattus norvegicus
Molecule
Arginase
EC
3.5.3.1
UniProt
P07824
Ligands
MN
Pockets
10 · best druggability 0.80

Structure

x-ray diffraction · resolution 2.94 · 1 distinct chain · 42% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CArginase (EC 3.5.3.1)protein31442% helix, 16% strandP07824

Ligands and binding sites

  • MN · Manganese (II) ion · metal · 3 copies · chains A, B, C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19330.800.8270empty
22410.570.7834empty
32540.560.7833empty
42970.550.7634empty
51060.480.8122empty

Interfaces

3 interfaces between chains.

  • A–C · 955 Ų buried · 13 hydrogen bonds · protein-protein
  • A–B · 954 Ų buried · 10 hydrogen bonds · protein-protein
  • B–C · 930 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 4RLA · Altering the binuclear manganese cluster of arginase diminishes thermostability and… · the same entry in another collection · chain A against A, TM-score 1.00
  • P07824 · AlphaFold monomer V2.0 prediction for arginase-1 (P07824) · a predicted model of the same protein · chain A against A, TM-score 1.00

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