MolNFT v1 · #169635 · protein
Protein engineering of xylose (glucose) isomerase from actinoplanes missouriensis. 1. crystallography and site-directed mutagenesis of metal binding sites
6XIM: “Protein engineering of xylose (glucose) isomerase from actinoplanes missouriensis. 1. crystallography and…”. X-ray diffraction, 2 ligands (XLS, MG). MolNFT v1 #169635 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6XIM
- Type
- protein
- Length
- 1,568 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P12851
- Ligands
- XLS, MG
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 392 | — | P12851 |
Ligands and binding sites
- XLS · D-xylose · ligand · 4 copies · chains A, B, C, D
- MG · Magnesium ion · metal · 8 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6XIM · Protein engineering of xylose (glucose) isomerase from actinoplanes missouriensis. 1.… · the same entry in another collection · chain A against A, TM-score 1.00
- P12851 · AlphaFold monomer V2.0 prediction for xylose isomerase (P12851) · 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 P12851
- Elsewhere: RCSB PDB 6XIM · PDBe 6XIM · UniProt P12851
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