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Crystal structure of the catalytic domain of human MMP12 complexed with acetohydroxamic acid at atomic resolution

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

PDB: 1Y93
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: HAE, CA, ZN
Pockets: 2 · best druggability 0.55

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	158	25% helix, 17% strand	P39900

Ligands and binding sites

HAE · Acetohydroxamic 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	140	0.55	0.82	27	HAE
2	54	0.31	0.76	16	empty

Compared structures

1Y93 · Crystal structure of the catalytic domain of human MMP12 complexed with acetohydroxamic… · 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 1Y93 · PDBe 1Y93 · UniProt P39900

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