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1.56 ångström structure of mature truncated human fibroblast collagenase

Analyse 1.56 ångström structure of mature truncated human fibroblast collagenase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1HFC
Type
protein
Length
157 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fibroblast collagenase
EC
3.4.24.7
UniProt
P03956
Ligands
PLH, ZN, CA
Pockets
1 · best druggability 0.39

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
AFibroblast collagenase (EC 3.4.24.7)protein15725% helix, 16% strandP03956

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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1660.390.8018ZN, PLH

Compared structures

  • 1HFC · 1.56 ångström structure of mature truncated human fibroblast collagenase · the same entry in another collection · chain A against A, TM-score 1.00
  • P03956 · AlphaFold monomer V2.0 prediction for interstitial collagenase (P03956) · a predicted model of the same protein · chain A against A, TM-score 0.99

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