MolNFT v1 · #20700 · protein

Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor nngh at 1.3 a resolution

1RMZ · Macrophage metalloelastase: “Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor nngh at 1.3 a resolution”. X-ray diffraction, 3 ligands (NGH, CA, ZN), 2 pockets (best druggability 0.56). MolNFT v1…

PDB: 1RMZ
Type: protein
Length: 159 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: NGH, CA, ZN
Pockets: 2 · best druggability 0.56

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Macrophage metalloelastase (EC 3.4.24.65)	protein	159	25% helix, 17% strand	P39900

Ligands and binding sites

NGH · N-isobutyl-N-[4-methoxyphenylsulfonyl]glycyl hydroxamic acid · 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

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	191	0.56	0.80	28	NGH
2	54	0.38	0.80	12	empty

Compared structures

1RMZ · 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 1RMZ · PDBe 1RMZ · UniProt P39900

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