Research workbench
Structure determination and rational mutagenesis reveal binding surface of immune adherence receptor, CR1 (CD35)
Analyse Structure determination and rational mutagenesis reveal binding surface of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GKG
- Type
- protein
- Length
- 136 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Complement receptor type 1
- UniProt
- P17927
Structure
solution nmr · 1 distinct chain · 0% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Complement receptor type 1 | protein | 136 | 0% helix, 27% strand | P17927 |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1GKG · Structure Determination and Rational Mutagenesis reveal binding surface of immune… · the same entry in another collection · chain A against A, TM-score 1.00
- P17927 · AlphaFold monomer V2.0 prediction for complement receptor type 1 (P17927) · a predicted model of the same protein · chain A against A, TM-score 0.83
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 P17927
- Elsewhere: RCSB PDB 1GKG · PDBe 1GKG · UniProt P17927
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