Research workbench
Novel inhibition mechanism of membrane metalloprotease by an exosite- swiveling conformational antibody
Analyse Novel inhibition mechanism of membrane metalloprotease by an exosite- swiveling… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QXU
- Type
- protein
- Length
- 450 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P50281
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | — | protein | 219 | — | — |
| H | — | protein | 220 | — | — |
| K | — | protein | 11 | — | P50281 |
Compared structures
- 4QXU · Novel Inhibition Mechanism of Membrane Metalloprotease by an Exosite-Swiveling… · the same entry in another collection · chain L against L, TM-score 1.00
- P50281 · AlphaFold monomer V2.0 prediction for matrix metalloproteinase-14 (P50281) · a predicted model of the same protein · chain K against A, TM-score 0.24
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 4QXU · PDBe 4QXU · UniProt P50281
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