Research workbench
Three-dimensional structure of porcine C5ADES*ARG from 1H nuclear magnetic resonance data
Analyse Three-dimensional structure of porcine C5ADES*ARG from 1H nuclear magnetic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1C5A
- Type
- protein
- Length
- 65 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Complement C5A anaphylatoxin
- UniProt
- P01032
Structure
solution nmr · 1 distinct chain · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Complement C5A anaphylatoxin | protein | 65 | 71% helix, 0% strand | P01032 |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1C5A · Three-dimensional structure of porcine C5ADES*ARG from 1H nuclear magnetic resonance data · the same entry in another collection · chain A against A, TM-score 1.00
- P01032 · AlphaFold monomer V2.0 prediction for complement C5A anaphylatoxin (P01032) · a predicted model of the same protein · chain A against A, TM-score 0.72
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 P01032
- Elsewhere: RCSB PDB 1C5A · PDBe 1C5A · UniProt P01032
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