Research workbench
Solution structure of the hemopexin-like domain of MMP12
Analyse Solution structure of the hemopexin-like domain of MMP12 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2JXY
- Type
- protein
- Length
- 194 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Macrophage metalloelastase
- EC
- 3.4.24.65
- UniProt
- P39900
- Ligands
- CA
- Pockets
- 4 · best druggability 0.65
Structure
solution nmr · 1 distinct chain · 4% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Macrophage metalloelastase (EC 3.4.24.65) | protein | 194 | 4% helix, 32% strand | P39900 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 249 | 0.65 | 0.82 | 32 | empty |
| 2 | 168 | 0.63 | 0.84 | 25 | empty |
| 3 | 87 | 0.53 | 0.84 | 14 | empty |
| 4 | 212 | 0.53 | 0.77 | 44 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2JXY · Solution structure of the hemopexin-like domain of MMP12 · the same entry in another collection · chain A against A, 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 2JXY · PDBe 2JXY · UniProt P39900
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