Research workbench
Crystal structure of the catalytic domain of membrane type 1 matrix metalloproteinase
Analyse Crystal structure of the catalytic domain of membrane type 1 matrix… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5H0U
- Type
- protein
- Length
- 176 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Matrix metalloproteinase-14; His-his-his-his-his-his
- EC
- 3.4.24.80
- UniProt
- P50281
- Ligands
- ZN, CA
- Pockets
- 1 · best druggability 0.51
Structure
x-ray diffraction · 2 distinct chains · 25% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Matrix metalloproteinase-14 (EC 3.4.24.80) | protein | 170 | 26% helix, 16% strand | P50281 |
| B | His-his-his-his-his-his | protein | 6 | 0% helix, 17% strand | — |
Ligands and binding sites
- ZN · Zinc ion · metal · 3 copies · chains A, B
- CA · Calcium ion · metal · 2 copies · chains A
- GOL · Glycerol · additive · 8 copies · chains A, B
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 78 | 0.51 | 0.84 | 19 | GOL |
Interfaces
1 interface between chains.
- A–B · 486 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 5H0U · Crystal structure of the catalytic domain of membrane type 1 matrix metalloproteinase · the same entry in another collection · chain A against A, TM-score 1.00
- P50281 · AlphaFold monomer V2.0 prediction for matrix metalloproteinase-14 (P50281) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P50281
- Elsewhere: RCSB PDB 5H0U · PDBe 5H0U · UniProt P50281
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