MolNFT v1 · #63163 · protein

Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor (S)-N-(2,3-dihydroxypropyl)-4-methoxy-N-(2- nitroso-2-OXOETHYL)BENZENESULFONAMIDE

3F15 · Macrophage metalloelastase: “Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor…”. X-ray diffraction, 3 ligands (HS1, CA, ZN), 1 pocket (best druggability 0.57). MolNFT v1 #63163 on GenesisL1: 3D…

PDB: 3F15
Type: protein
Length: 158 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Macrophage metalloelastase
EC: 3.4.24.65
UniProt: P39900
Ligands: HS1, CA, ZN
Pockets: 1 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Macrophage metalloelastase (EC 3.4.24.65)	protein	158	26% helix, 17% strand	P39900

Ligands and binding sites

HS1 · 2-[[(2S)-2,3-dihydroxypropyl]-(4-methoxyphenyl)sulfonyl-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	145	0.57	0.82	21	HS1

Compared structures

3F15 · 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 3F15 · PDBe 3F15 · UniProt P39900

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