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Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin

Analyse Crystal structure analysis of the peptide amidase pam in complex with the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1M21
Type
protein
Length
982 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Peptide amidase; Chymostatin
EC
3.5.1.-
UniProt
Q8RJN5
Pockets
6 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BPeptide amidase (EC 3.5.1.-)protein48740% helix, 15% strandQ8RJN5
C, DChymostatinprotein40% helix, 0% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11000.610.8830empty
21550.540.8042empty
32240.520.7650empty
4820.420.8014empty
5560.370.8011empty

Interfaces

3 interfaces between chains.

  • A–C · 493 Ų buried · 6 hydrogen bonds · protein-protein
  • B–D · 491 Ų buried · 5 hydrogen bonds · protein-protein
  • A–B · 28 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (nonstandard).

Compared structures

  • 1M21 · Crystal structure analysis of the peptide amidase PAM in complex with the competitive… · the same entry in another collection · chain A against A, TM-score 1.00

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