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Crystal structure of helicobacter pylori arginase

Analyse Crystal structure of helicobacter pylori arginase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4G3H
Type
protein
Length
1,216 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Arginase (rocf)
UniProt
O25949
Ligands
MN
Pockets
11 · best druggability 0.82

Structure

x-ray diffraction · 4 distinct chains · 46% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AArginase (rocf)protein30146% helix, 18% strandO25949
BArginase (rocf)protein30546% helix, 18% strandO25949
CArginase (rocf)protein31046% helix, 17% strandO25949
DArginase (rocf)protein30046% helix, 17% strandO25949

Ligands and binding sites

  • 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

11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19510.820.8477empty
28930.820.8481empty
31960.680.8632empty
43060.620.7943empty
52050.590.8134empty

Interfaces

5 interfaces between chains.

  • A–D · 689 Ų buried · 4 hydrogen bonds · protein-protein
  • A–C · 608 Ų buried · 9 hydrogen bonds · protein-protein
  • B–D · 603 Ų buried · 11 hydrogen bonds · protein-protein
  • C–D · 345 Ų buried · 1 hydrogen bond · protein-protein
  • A–B · 336 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 4G3H · Crystal structure of helicobacter pylori arginase · the same entry in another collection · chain A against A, TM-score 1.00

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