Research workbench
CD1C in complex with pm (phosphomycoketide)
Analyse CD1C in complex with pm (phosphomycoketide) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ONO
- Type
- protein
- Length
- 374 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P61769, P29017, P29016
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 374 | — | P61769, P29017, P29016 |
Compared structures
- 4ONO · CD1c in complex with PM (phosphomycoketide) · the same entry in another collection · chain A against A, TM-score 1.00
- P29017 · AlphaFold monomer V2.0 prediction for T-cell surface glycoprotein CD1C (P29017) · a predicted model of the same protein · chain A against A, TM-score 0.69
- P29016 · AlphaFold monomer V2.0 prediction for T-cell surface glycoprotein CD1B (P29016) · a predicted model of the same protein · chain A against A, TM-score 0.69
- P61769 · AlphaFold monomer V2.0 prediction for beta-2-microglobulin (P61769) · a predicted model of the same protein · chain A against A, TM-score 0.26
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 P61769
- Every structure of UniProt P29017
- Every structure of UniProt P29016
- Elsewhere: RCSB PDB 4ONO · PDBe 4ONO · UniProt P61769 · UniProt P29017 · UniProt P29016
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