Research workbench
Crystal structure of the catalytic domain of mmp-13 complexed with way-344
Analyse Crystal structure of the catalytic domain of mmp-13 complexed with way-344 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PJT
- Type
- protein
- Length
- 646 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P45452
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 162 | — | P45452 |
| B | — | protein | 164 | — | P45452 |
| C | — | protein | 159 | — | P45452 |
| D | — | protein | 161 | — | P45452 |
Compared structures
- 2PJT · Crystal structure of the catalytic domain of MMP-13 complexed with WAY-344 · the same entry in another collection · chain C against C, TM-score 1.00
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 2PJT · PDBe 2PJT · UniProt P45452
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