MolNFT v1 · #27933 · protein
The role of the divalent metal ion in sugar binding, ring opening, and isomerization by D-xylose isomerase: replacement of a catalytic metal by an amino-acid
1XYL: “The role of the divalent metal ion in sugar binding, ring opening, and isomerization by D-xylose isomerase…”. X-ray diffraction. MolNFT v1 #27933 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1XYL
- Type
- protein
- Length
- 772 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P15587
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 386 | — | P15587 |
Compared structures
- 1XYL · The role of the divalent metal ion in sugar binding, ring opening, and isomerization by… · the same entry in another collection · chain A against A, TM-score 1.00
- P15587 · AlphaFold monomer V2.0 prediction for xylose isomerase (P15587) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 P15587
- Elsewhere: RCSB PDB 1XYL · PDBe 1XYL · UniProt P15587
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