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Crystal structure of arginase from zymomonas mobilis ZM4

Analyse Crystal structure of arginase from zymomonas mobilis ZM4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6KSY
Type
protein
Length
1,145 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ARGINASE/AGMATINASE/FORMIMINOGLUTAMASE
UniProt
Q5NQE9
Ligands
ZN
Pockets
9 · best druggability 0.69

Structure

x-ray diffraction · 4 distinct chains · 41% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AARGINASE/AGMATINASE/FORMIMINOGLUTAMASEprotein28641% helix, 17% strandQ5NQE9
BARGINASE/AGMATINASE/FORMIMINOGLUTAMASEprotein28941% helix, 16% strandQ5NQE9
CARGINASE/AGMATINASE/FORMIMINOGLUTAMASEprotein28442% helix, 16% strandQ5NQE9
DARGINASE/AGMATINASE/FORMIMINOGLUTAMASEprotein28641% helix, 17% strandQ5NQE9

Ligands and binding sites

  • ZN · Zinc 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

9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14990.690.7965empty
25460.690.7959empty
31490.580.8322empty
41430.560.8222empty
51560.550.8024empty

Interfaces

4 interfaces between chains.

  • A–D · 2165 Ų buried · 16 hydrogen bonds · protein-protein
  • B–C · 561 Ų buried · 7 hydrogen bonds · protein-protein
  • A–C · 531 Ų buried · 7 hydrogen bonds · protein-protein
  • A–B · 156 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 6KSY · Crystal structure of arginase from Zymomonas mobilis ZM4 · the same entry in another collection · chain A against A, TM-score 1.00

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