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Crystal structure of MMP12 in complex with inhibitor BE7.
Analyse Crystal structure of MMP12 in complex with inhibitor BE7. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EKN
- Type
- protein
- Length
- 159 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.2
- Source
- Homo sapiens
- Molecule
- Macrophage metalloelastase
- EC
- 3.4.24.65
- UniProt
- P39900
- Ligands
- B9N, CA, ZN
- Pockets
- 2 · best druggability 0.58
Structure
x-ray diffraction · resolution 1.2 · 1 distinct chain · 25% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Macrophage metalloelastase (EC 3.4.24.65) | protein | 159 | 25% helix, 17% strand | P39900 |
Ligands and binding sites
- B9N · (2~{S})-2-[2-[4-(4-methoxyphenyl) phenyl]sulfonylphenyl]pentanedioic acid · ligand · chains A
- CA · Calcium ion · metal · 3 copies · chains A
- ZN · Zinc ion · metal · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · 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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 158 | 0.58 | 0.82 | 25 | B9N |
| 2 | 81 | 0.35 | 0.75 | 22 | empty |
Compared structures
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 6EKN · PDBe 6EKN · UniProt P39900
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