Research workbench
Collagenase-3 (mmp-13) C-terminal hemopexin-like domain
Analyse Collagenase-3 (mmp-13) C-terminal hemopexin-like domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PEX
- Type
- protein
- Length
- 192 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Collagenase-3
- EC
- 3.4.24.-
- UniProt
- P45452
- Ligands
- CA, CL, SO4
- Pockets
- 4 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Collagenase-3 (EC 3.4.24.-) | protein | 192 | 7% helix, 42% strand | P45452 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A
- CL · Chloride ion · ion · 2 copies · chains A
- SO4 · Sulfate ion · ion · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 115 | 0.52 | 0.81 | 22 | CL |
| 2 | 75 | 0.38 | 0.77 | 13 | empty |
| 3 | 51 | 0.36 | 0.79 | 17 | empty |
| 4 | 82 | 0.35 | 0.75 | 16 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 P45452
- Elsewhere: RCSB PDB 1PEX · PDBe 1PEX · UniProt P45452
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