Research workbench
Helicobacter pylori formamidase amif contains a fine-tuned cysteine- glutamate-lysine catalytic triad
Analyse Helicobacter pylori formamidase amif contains a fine-tuned cysteine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2E2K
- Type
- protein
- Length
- 1,881 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O25836
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 313 | — | O25836 |
| B | — | protein | 314 | — | O25836 |
| C | — | protein | 314 | — | O25836 |
| D | — | protein | 311 | — | O25836 |
| E | — | protein | 315 | — | O25836 |
| F | — | protein | 314 | — | O25836 |
Compared structures
- 2E2K · Helicobacter pylori formamidase AmiF contains a fine-tuned cysteine-glutamate-lysine… · the same entry in another collection · chain F against F, TM-score 1.00
- O25836 · AlphaFold monomer V2.0 prediction for formamidase (O25836) · a predicted model of the same protein · chain C 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 O25836
- Elsewhere: RCSB PDB 2E2K · PDBe 2E2K · UniProt O25836
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