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Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor nngh

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: 5LAB
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 · 26% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Macrophage metalloelastase (EC 3.4.24.65)	protein	159	26% 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	0.79	28	NGH
2	56	0.37	0.79	12	empty

Compared structures

5LAB · Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor NNGH · 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 5LAB · PDBe 5LAB · UniProt P39900

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