Research workbench
Crystal structure of human CD45 extracellular region, domains D1-D3
Analyse Crystal structure of human CD45 extracellular region, domains D1-D3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FN6
- Type
- protein
- Length
- 252 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receptor-type tyrosine-protein phosphatase C
- EC
- 3.1.3.48
- UniProt
- P08575
- Ligands
- NAG
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor-type tyrosine-protein phosphatase C (EC 3.1.3.48) | protein | 252 | 6% helix, 53% strand | P08575 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 7 disulfide, 5 glycan (disulfide, N-glycosylation).
Compared structures
- 5FN6 · Crystal structure of human CD45 extracellular region, domains d1-d3 · the same entry in another collection · chain A against A, TM-score 1.00
- P08575 · AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein phosphatase C… · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P08575
- Elsewhere: RCSB PDB 5FN6 · PDBe 5FN6 · UniProt P08575
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