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Crystal structure of the catalytic domain of human fibroblast stromelysin-1 inhibited with thiadiazole inhibitor pnu-141803

Analyse Crystal structure of the catalytic domain of human fibroblast stromelysin-1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2USN
Type: protein
Length: 165 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Stromelysin-1
EC: 3.4.24.17
UniProt: P08254
Ligands: IN8, ZN, CA
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Stromelysin-1 (EC 3.4.24.17)	protein	165	28% helix, 18% strand	P08254

Ligands and binding sites

IN8 · [2-(5-mercapto-[1,3,4]thiadiazol-2-ylcarbamoyl)-1-phenyl-ethyl]-carbamic acid benzyl ester · ligand · chains A
ZN · Zinc ion · metal · 3 copies · chains A
CA · Calcium ion · metal · 3 copies · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	70	0.30	0.73	18	IN8

Compared structures

2USN · Crystal structure of the catalytic domain of human fibroblast stromelysin-1 inhibited… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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Every structure of UniProt P08254
Elsewhere: RCSB PDB 2USN · PDBe 2USN · UniProt P08254

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