Research workbench
Orientation in solution of mmp-3 catalytic domain and N-timp-1 from residual dipolar couplings
Analyse Orientation in solution of mmp-3 catalytic domain and N-timp-1 from residual… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OO9
- Type
- protein
- Length
- 294 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Stromelysin-1; Metalloproteinase inhibitor 1
- EC
- 3.4.24.17
- UniProt
- P08254, P01033
- Pockets
- 4 · best druggability 0.68
Structure
solution nmr · 2 distinct chains · 24% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Stromelysin-1 (EC 3.4.24.17) | protein | 168 | 25% helix, 18% strand | P08254 |
| B | Metalloproteinase inhibitor 1 | protein | 126 | 22% helix, 34% strand | P01033 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 223 | 0.68 | 0.85 | 29 | empty |
| 2 | 108 | 0.62 | 0.88 | 19 | empty |
| 3 | 87 | 0.45 | 0.80 | 17 | empty |
| 4 | 164 | 0.45 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 990 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1OO9 · Orientation in Solution of MMP-3 Catalytic Domain and N-TIMP-1 from Residual Dipolar… · the same entry in another collection · chain A against A, TM-score 1.00
- P08254 · AlphaFold monomer V2.0 prediction for stromelysin-1 (P08254) · a predicted model of the same protein · chain A against A, TM-score 0.95
- P01033 · AlphaFold monomer V2.0 prediction for metalloproteinase inhibitor 1 (P01033) · a predicted model of the same protein · chain B against A, TM-score 0.93
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 P08254
- Every structure of UniProt P01033
- Elsewhere: RCSB PDB 1OO9 · PDBe 1OO9 · UniProt P08254 · UniProt P01033
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