MolNFT v1 · #14855 · protein
Matrilysin complexed with hydroxamate inhibitor
1MMQ: “Matrilysin complexed with hydroxamate inhibitor”. X-ray diffraction, 3 ligands (RRS, ZN, CA), 1 pocket (best druggability 0.43). MolNFT v1 #14855 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1MMQ
- Type
- protein
- Length
- 166 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Matrilysin
- EC
- 3.4.24.23
- UniProt
- P09237
- Ligands
- RRS, ZN, CA
- Pockets
- 1 · best druggability 0.43
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Matrilysin (EC 3.4.24.23) | protein | 166 | 25% helix, 17% strand | P09237 |
Ligands and binding sites
- RRS · N4-hydroxy-2-isobutyl-N1-(9-oxo-1,8-diaza-tricyclo[10.6.1.013,18]nonadeca-12(19),13,15,17-tetraen-10-yl)-succinamide · ligand · chains A
- ZN · Zinc ion · metal · 2 copies · chains A
- CA · Calcium 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 77 | 0.43 | 0.81 | 19 | ZN, RRS |
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 P09237
- Elsewhere: RCSB PDB 1MMQ · PDBe 1MMQ · UniProt P09237
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