Research workbench
Solution structure of cfafp-501
Analyse Solution structure of cfafp-501 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Z2F
- Type
- protein
- Length
- 121 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Antifreeze protein isoform 501
- UniProt
- Q9GSA6
Structure
solution nmr · 1 distinct chain · 0% helix, 60% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Antifreeze protein isoform 501 | protein | 121 | 0% helix, 60% strand | Q9GSA6 |
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 1Z2F · solution structure of CfAFP-501 · the same entry in another collection · chain A against A, TM-score 1.00
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 Q9GSA6
- Elsewhere: RCSB PDB 1Z2F · PDBe 1Z2F · UniProt Q9GSA6
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