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Structure of human neutrophil collagenase reveals large S1' specificity pocket

Analyse Structure of human neutrophil collagenase reveals large S1' specificity pocket in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1MNC
Type
protein
Length
158 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Neutrophil collagenase
EC
3.4.24.7
UniProt
P22894
Ligands
PLH, ZN, CA
Pockets
1 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANeutrophil collagenase (EC 3.4.24.7)protein15825% helix, 16% strandP22894

Ligands and binding sites

  • PLH · Methylamino-phenylalanyl-leucyl-hydroxamic acid · ligand · chains A
  • ZN · Zinc ion · metal · 2 copies · chains A
  • CA · Calcium ion · metal · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11280.560.8323PLH

Compared structures

  • 1MNC · Structure of human neutrophil collagenase reveals large S1' specificity pocket · the same entry in another collection · chain A against A, TM-score 1.00
  • P22894 · AlphaFold monomer V2.0 prediction for neutrophil collagenase (P22894) · a predicted model of the same protein · chain A against A, TM-score 0.98

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