Research workbench
Transient collagen triple helix binding to a key metalloproteinase in invasion and development: spin labels to structure
Analyse Transient collagen triple helix binding to a key metalloproteinase in invasion… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MQS
- Type
- protein
- Length
- 301 residues
- Chains
- 4
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P50281
Structure
solution nmr · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 196 | — | P50281 |
| B, C | — | protein | 36 | — | — |
| D | — | protein | 33 | — | — |
Compared structures
- 2MQS · Transient Collagen Triple Helix Binding to a Key Metalloproteinase in Invasion and… · the same entry in another collection · chain D against D, 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 2MQS · PDBe 2MQS · UniProt P50281
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