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X-ray crystallographic structure model of lactococcus lactis prolidase mutant D36S

Analyse X-ray crystallographic structure model of lactococcus lactis prolidase mutant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7N02
Type
protein
Length
724 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Aminopeptidase P family protein
EC
3.4.13.9
UniProt
A8WBX8
Ligands
MN
Pockets
6 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BAminopeptidase P family protein (EC 3.4.13.9)protein36237% helix, 23% strandA8WBX8

Ligands and binding sites

  • MN · Manganese (II) ion · metal · 4 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13580.620.7836empty
23220.540.7427empty
32200.500.7626empty
41460.460.7721empty
51080.440.7817empty

Interfaces

1 interface between chains.

  • A–B · 859 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 7N02 · X-ray crystallographic structure model of Lactococcus lactis prolidase mutant D36S · the same entry in another collection · chain A against A, TM-score 1.00

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