MolNFT v1 · #17390 · protein
Ternary enzyme-product-inhibitor complexes of human MMP12
1OS2 · Macrophage metalloelastase: “Ternary enzyme-product-inhibitor complexes of human MMP12”. X-ray diffraction, 4 ligands (HAE, CA, ZN), 11 pockets (best druggability 0.76). MolNFT v1 #17390 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1OS2
- Type
- protein
- Length
- 990 residues
- Chains
- 6
- 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, AZI
- Pockets
- 11 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Macrophage metalloelastase (EC 3.4.24.65) | protein | 165 | 24% helix, 17% strand | P39900 |
Ligands and binding sites
- HAE · Acetohydroxamic acid · ligand · 2 copies · chains A, D
- CA · Calcium ion · metal · 18 copies · chains A, B, C, D, E, F
- ZN · Zinc ion · metal · 12 copies · chains A, B, C, D, E, F
- AZI · Azide ion · ion · 2 copies · chains B, C, E, F
- ACT · Acetate ion · additive · 2 copies · chains A, B, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1017 | 0.76 | 0.79 | 78 | ACT |
| 2 | 372 | 0.76 | 0.86 | 55 | empty |
| 3 | 1035 | 0.75 | 0.78 | 75 | ACT |
| 4 | 473 | 0.67 | 0.79 | 56 | HAE |
| 5 | 401 | 0.63 | 0.78 | 54 | ZN, HAE |
Interfaces
7 interfaces between chains.
- B–E · 576 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 574 Ų buried · 10 hydrogen bonds · protein-protein
- E–F · 573 Ų buried · 10 hydrogen bonds · protein-protein
- D–E · 498 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 492 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 1OS2 · Ternary enzyme-product-inhibitor complexes of human MMP12 · the same entry in another collection · chain F against F, 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 1OS2 · PDBe 1OS2 · UniProt P39900
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.