Research workbench
NMR solution structure of human pancreatitis-associated protein
Analyse NMR solution structure of human pancreatitis-associated protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GO0
- Type
- protein
- Length
- 137 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Regenerating islet-derived protein 3 alpha
- UniProt
- Q06141
Structure
solution nmr · 1 distinct chain · 16% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Regenerating islet-derived protein 3 alpha | protein | 137 | 16% helix, 31% strand | Q06141 |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 2GO0 · NMR solution structure of human pancreatitis-associated protein · the same entry in another collection · chain A against A, TM-score 1.00
- Q06141 · AlphaFold monomer V2.0 prediction for regenerating islet-derived protein 3-alpha (Q06141) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 Q06141
- Elsewhere: RCSB PDB 2GO0 · PDBe 2GO0 · UniProt Q06141
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