MolNFT v1 · #119487 · protein
Structure of fae solved by sad from data collected by direct data collection (ddc) using the esrf robodiff goniometer
5FXM: “Structure of fae solved by sad from data collected by direct data collection (ddc) using the esrf robodiff…”. X-ray diffraction. MolNFT v1 #119487 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5FXM
- Type
- protein
- Length
- 283 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P51584
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 283 | — | P51584 |
Compared structures
- 5FXM · Structure of FAE solved by SAD from data collected by Direct Data Collection (DDC) using… · the same entry in another collection · chain A against A, TM-score 1.00
- P51584 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase Y (P51584) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P51584
- Elsewhere: RCSB PDB 5FXM · PDBe 5FXM · UniProt P51584
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