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Structure of karilysin mmp-like catalytic domain in complex with inhibitory tetrapeptide swfp

Analyse Structure of karilysin mmp-like catalytic domain in complex with inhibitory… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4IN9
Type: protein
Length: 166 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Karilysin protease; Peptide ser-TRP-phe-pro
UniProt: D0EM77
Ligands: ZN, K, NA

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Karilysin protease	protein	162	29% helix, 20% strand	D0EM77
B	Peptide ser-TRP-phe-pro	protein	4	0% helix, 0% strand	—

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B
K · Potassium ion · metal · chains A
NA · Sodium ion · metal · chains A
GOL · Glycerol · additive · 5 copies · chains A, B

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

Interfaces

1 interface between chains.

A–B · 396 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

4IN9 · Structure of karilysin MMP-like catalytic domain in complex with inhibitory tetrapeptide… · the same entry in another collection · chain A against A, TM-score 1.00
D0EM77 · AlphaFold monomer V2.0 prediction for karilysin (D0EM77) · a predicted model of the same protein · chain A against A, TM-score 0.96

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt D0EM77
Elsewhere: RCSB PDB 4IN9 · PDBe 4IN9 · UniProt D0EM77

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