MolNFT v1 · #114385 · protein
The active site of O-glcnac transferase imposes constraints on substrate sequence
5BNW: “The active site of O-glcnac transferase imposes constraints on substrate sequence”. X-ray diffraction. MolNFT v1 #114385 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5BNW
- Type
- protein
- Length
- 701 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O15294
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 694 | — | O15294 |
| D | — | protein | 7 | — | — |
Compared structures
- 5BNW · The active site of O-GlcNAc transferase imposes constraints on substrate sequence · the same entry in another collection · chain A against A, TM-score 1.00
- O15294 · AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine-- peptide… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 O15294
- Elsewhere: RCSB PDB 5BNW · PDBe 5BNW · UniProt O15294
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