Research workbench
Cysteine deleted protegrin-1 (cdp-1): anti-bacterial activity, outer- membrane disruption and selectivity
Analyse Cysteine deleted protegrin-1 (cdp-1): anti-bacterial activity, outer- membrane… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MQ5
- Type
- protein
- Length
- 10 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- LR10 peptide from cysteine deleted protegrin-1
Structure
solution nmr · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | LR10 peptide from cysteine deleted protegrin-1 | protein | 10 | 0% helix, 0% strand | — |
Compared structures
- 2MQ5 · Cysteine Deleted Protegrin-1 (CDP-1): Anti-bacterial Activity, Outer-Membrane Disruption… · 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
- Elsewhere: RCSB PDB 2MQ5 · PDBe 2MQ5
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