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Solution structure of the catalytic fragment of human collagenase-3 (mmp-13) complexed with a hydroxamic acid inhibitor
Analyse Solution structure of the catalytic fragment of human collagenase-3 (mmp-13)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FLS
- Type
- protein
- Length
- 158 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P45452
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 158 | — | P45452 |
Compared structures
- 1FLS · Solution structure of the catalytic fragment of human collagenase-3 (mmp-13) complexed… · the same entry in another collection · chain A against A, TM-score 1.00
- P45452 · AlphaFold monomer V2.0 prediction for collagenase 3 (P45452) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 1FLS · PDBe 1FLS · UniProt P45452
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