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Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor 4-fluoro-N-(2-hydroxyethyl)-N-(2-nitroso-2- OXOETHYL)BENZENESULFONAMIDE

Analyse Crystal structure of the catalytic domain of human MMP12 complexed with the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3F18
Type: protein
Length: 158 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Macrophage metalloelastase
UniProt: P39900
Ligands: HS5, CA, ZN
Pockets: 1 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Macrophage metalloelastase	protein	158	25% helix, 17% strand	P39900

Ligands and binding sites

HS5 · 2-[(4-fluorophenyl)sulfonyl-(2-hydroxyethyl)amino]-N-oxo-ethanamide · ligand · chains A
CA · Calcium ion · metal · 3 copies · chains A
ZN · Zinc ion · metal · 2 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	147	0.54	0.80	25	ZN, HS5

Compared structures

3F18 · Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor… · the same entry in another collection · chain A against A, TM-score 1.00

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 P39900
Elsewhere: RCSB PDB 3F18 · PDBe 3F18 · UniProt P39900

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