Research workbench
NMR solution structure of the pro form of human matrilysin (prommp-7) in complex with anionic membrane
Analyse NMR solution structure of the pro form of human matrilysin (prommp-7) in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MZI
- Type
- protein
- Length
- 248 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Matrilysin
- EC
- 3.4.24.23
- UniProt
- P09237
- Ligands
- PX4, C3S, CA, ZN
- Pockets
- 2 · best druggability 0.77
Structure
solution nmr · 1 distinct chain · 27% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Matrilysin (EC 3.4.24.23) | protein | 248 | 27% helix, 11% strand | P09237 |
Ligands and binding sites
- PX4 · 1,2-dimyristoyl-sn-glycero-3-phosphocholine · ligand · 126 copies · chains A
- C3S · Cholest-5-en-3-yl hydrogen sulfate · ligand · 6 copies · chains A
- CA · Calcium ion · metal · 2 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 573 | 0.77 | 0.83 | 84 | empty |
| 2 | 185 | 0.51 | 0.77 | 28 | empty |
Compared structures
- 2MZI · NMR Solution Structure of the PRO Form of Human Matrilysin (proMMP-7) in Complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- P09237 · AlphaFold monomer V2.0 prediction for matrilysin (P09237) · a predicted model of the same protein · chain A against A, TM-score 0.76
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 2MZI · PDBe 2MZI · UniProt P09237
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