Research workbench
Human MMP12 catalytic domain in complex with AP280
Analyse Human MMP12 catalytic domain in complex with AP280 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6RD0
- Type
- protein
- Length
- 159 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
- K0Q, HAE, CA, ZN
- Pockets
- 2 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Macrophage metalloelastase (EC 3.4.24.65) | protein | 159 | 24% helix, 17% strand | P39900 |
Ligands and binding sites
- K0Q · ~{N}-[2-(1~{H}-indol-3-yl)ethyl]-2-(3-oxidanyl-2-oxidanylidene-pyridin-1-yl)ethanamide · ligand · chains A
- 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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 151 | 0.58 | 0.82 | 25 | ZN, K0Q, HAE |
| 2 | 91 | 0.36 | 0.75 | 21 | 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 6RD0 · PDBe 6RD0 · UniProt P39900
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