Research workbench
Solution structure of the catalytic domain of human collagenase-3 (mmp-13) complexed to a potent non-peptidic sulfonamide inhibitor
Analyse Solution structure of the catalytic domain of human collagenase-3 (mmp-13)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EUB
- Type
- protein
- Length
- 171 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Collagenase 3
- EC
- 3.4.24.-
- UniProt
- P45452
- Ligands
- HAV, 3MP, MSB, ZN, CA
- Pockets
- 2 · best druggability 0.46
Structure
solution nmr · 1 distinct chain · 23% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Collagenase 3 (EC 3.4.24.-) | protein | 171 | 23% helix, 16% strand | P45452 |
Ligands and binding sites
- HAV · Hydroxyaminovaline · ligand · chains A
- 3MP · 3-methylpyridine · ligand · chains A
- MSB · 1-methyloxy-4-sulfone-benzene · 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
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 88 | 0.46 | 0.81 | 20 | HAV, MSB |
| 2 | 65 | 0.42 | 0.81 | 19 | empty |
Compared structures
- 1EUB · Solution structure of the catalytic domain of human collagenase-3 (mmp-13) complexed to a… · the same entry in another collection · chain A against A, TM-score 1.00
- P45452 · AlphaFold monomer V2.0 prediction for collagenase 3 (P45452) · a predicted model of the same protein · chain A against A, TM-score 0.75
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 P45452
- Elsewhere: RCSB PDB 1EUB · PDBe 1EUB · UniProt P45452
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