Research workbench
NMR solution structure of the activation domain of human procarboxypeptidase A2
Analyse NMR solution structure of the activation domain of human procarboxypeptidase A2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1O6X
- Type
- protein
- Length
- 81 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Procarboxypeptidase A2
- EC
- 3.4.17.15
- UniProt
- P48052
Structure
solution nmr · 1 distinct chain · 31% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Procarboxypeptidase A2 (EC 3.4.17.15) | protein | 81 | 31% helix, 20% strand | P48052 |
Compared structures
- 1O6X · NMR solution structure of the activation domain of human procarboxypeptidase A2 · the same entry in another collection · chain A against A, TM-score 1.00
- P48052 · AlphaFold monomer V2.0 prediction for carboxypeptidase A2 (P48052) · a predicted model of the same protein · chain A against A, TM-score 0.78
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 P48052
- Elsewhere: RCSB PDB 1O6X · PDBe 1O6X · UniProt P48052
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