Research workbench
Complex of pro-leu-gly-hydroxylamine with the catalytic domain of matrix metallo proteinase-8 (PHE79 form)
Analyse Complex of pro-leu-gly-hydroxylamine with the catalytic domain of matrix… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JAN
- Type
- protein
- Length
- 167 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P22894
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 164 | — | P22894 |
| I | — | protein | 3 | — | — |
Compared structures
- 1JAN · Complex of pro-leu-gly-hydroxylamine with the catalytic domain of matrix metallo… · the same entry in another collection · chain A against A, TM-score 1.00
- P22894 · AlphaFold monomer V2.0 prediction for neutrophil collagenase (P22894) · 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 P22894
- Elsewhere: RCSB PDB 1JAN · PDBe 1JAN · UniProt P22894
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