MolNFT v1 · #41914 · protein

Solution structure of the wild-type catalytic domain of human matrix metalloproteinase 12 (mmp-12) in complex with a tight-binding inhibitor

2K2G · Macrophage metalloelastase: “Solution structure of the wild-type catalytic domain of human matrix metalloproteinase 12 (mmp-12) in complex…”. Solution nmr, 2 ligands (DSV, ZN), 5 pockets (best druggability 0.70). MolNFT v1 #41914 on…

PDB: 2K2G
Type: protein
Length: 165 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Macrophage metalloelastase
EC: 3.4.24.65
UniProt: P39900
Ligands: DSV, ZN
Pockets: 5 · best druggability 0.70

Structure

solution nmr · 1 distinct chain · 26% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Macrophage metalloelastase (EC 3.4.24.65)	protein	165	26% helix, 8% strand	P39900

Ligands and binding sites

DSV · N-(dibenzo[b,d]thiophen-3-ylsulfonyl)-L-valine · ligand · 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

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	88	0.70	0.93	24	empty
2	102	0.68	0.91	22	empty
3	107	0.57	0.84	22	empty
4	96	0.39	0.77	19	DSV
5	70	0.36	0.77	19	empty

Compared structures

2K2G · Solution structure of the wild-type catalytic domain of human matrix metalloproteinase 12… · 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 2K2G · PDBe 2K2G · UniProt P39900

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