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Catalytic domain of human mmp-12 complexed with hydroxamic acid and paramethoxy-sulfonyl amide

Analyse Catalytic domain of human mmp-12 complexed with hydroxamic acid and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3LKA
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, M4S, CA, ZN
Pockets: 1 · best druggability 0.58

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

HAE · Acetohydroxamic acid · ligand · chains A
M4S · 4-methoxybenzenesulfonamide · 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	151	0.58	0.82	26	ZN, HAE, M4S

Compared structures

3LKA · Catalytic domain of human MMP-12 complexed with hydroxamic acid and paramethoxy-sulfonyl… · 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 3LKA · PDBe 3LKA · UniProt P39900

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