Research workbench
Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor
Analyse Structure of the catalytic domain of fibroblast collagenase complexed with an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CGL
- Type
- protein
- Length
- 327 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P03956
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 169 | — | P03956 |
| B | — | protein | 158 | — | P03956 |
Compared structures
- 1CGL · Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor · the same entry in another collection · chain A against A, TM-score 0.99
- P03956 · AlphaFold monomer V2.0 prediction for interstitial collagenase (P03956) · a predicted model of the same protein · chain B 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 P03956
- Elsewhere: RCSB PDB 1CGL · PDBe 1CGL · UniProt P03956
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