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Crystal structure of N-carbamoylsarcosine amidase from thermoplasma acidophilum

Analyse Crystal structure of N-carbamoylsarcosine amidase from thermoplasma acidophilum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3EEF
Type
protein
Length
346 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
N-carbamoylsarcosine amidase related protein
EC
3.5.1.59
UniProt
Q9HKY9
Ligands
ZN
Pockets
3 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BN-carbamoylsarcosine amidase related protein (EC 3.5.1.59)protein17335% helix, 24% strandQ9HKY9

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1830.620.8919empty
21220.560.8318empty
31260.560.8218empty

Interfaces

1 interface between chains.

  • A–B · 1121 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

  • 3EEF · Crystal structure of N-carbamoylsarcosine amidase from thermoplasma acidophilum · the same entry in another collection · chain A against A, TM-score 1.00

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