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MolNFT v1 · #64396 · protein

Crystal structure of a ld-carboxypeptidase a (SARO_1426) from novosphingobium aromaticivorans dsm at 1.89 a resolution

3G23: “Crystal structure of a ld-carboxypeptidase a (SARO_1426) from novosphingobium aromaticivorans dsm at 1.89 a…”. X-ray diffraction, 2 ligands (UNL, SO4), 3 pockets (best druggability 0.73). MolNFT v1 #64396 on GenesisL1: 3D structure…

PDB
3G23
Type
protein
Length
540 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ld-carboxypeptidase a
UniProt
Q2G8F3
Ligands
UNL, SO4
Pockets
3 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BLd-carboxypeptidase aprotein27039% helix, 19% strandQ2G8F3

Ligands and binding sites

  • UNL · Unknown ligand · ligand · chains A, B
  • SO4 · Sulfate ion · ion · 17 copies · chains A, B
  • GOL · Glycerol · additive · 8 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17710.730.7875SO4, GOL, UNL
21090.450.7919GOL
3540.380.8017empty

Interfaces

1 interface between chains.

  • A–B · 1404 Ų buried · 24 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

  • 3G23 · Crystal structure of a ld-carboxypeptidase a (saro_1426) from novosphingobium… · the same entry in another collection · chain A against A, TM-score 1.00

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