Research workbench
Human O-glcnac transferase (ogt) in complex with udp and glycopeptide
Analyse Human O-glcnac transferase (ogt) in complex with udp and glycopeptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AY5
- Type
- protein
- Length
- 2,836 residues
- Chains
- 8
- 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, B, C, D | — | protein | 698 | — | O15294 |
| I, J, K, L | — | protein | 11 | — | — |
Compared structures
- 4AY5 · Human O-GlcNAc transferase (OGT) in complex with UDP and glycopeptide · the same entry in another collection · chain L against L, 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 0.96
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 O15294
- Elsewhere: RCSB PDB 4AY5 · PDBe 4AY5 · UniProt O15294
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