Research workbench
Crystal structure of the MT1-mmp-timp-2 complex
Analyse Crystal structure of the MT1-mmp-timp-2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BUV
- Type
- protein
- Length
- 358 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P50281, P16368
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| M | — | protein | 174 | — | P50281 |
| T | — | protein | 184 | — | P16368 |
Compared structures
- 1BUV · Crystal structure of the MT1-mmp-timp-2 complex · the same entry in another collection · chain M against M, TM-score 1.00
- P50281 · AlphaFold monomer V2.0 prediction for matrix metalloproteinase-14 (P50281) · a predicted model of the same protein · chain M against A, TM-score 0.94
- P16368 · AlphaFold monomer V2.0 prediction for metalloproteinase inhibitor 2 (P16368) · a predicted model of the same protein · chain T against A, TM-score 0.89
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
- Every structure of UniProt P16368
- Elsewhere: RCSB PDB 1BUV · PDBe 1BUV · UniProt P50281 · UniProt P16368
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