Research workbench
Ggvlvn segment from human prostatic acid phosphatase residues 260-265, involved in semen-derived enhancer of viral infection
Analyse Ggvlvn segment from human prostatic acid phosphatase residues 260-265, involved… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PPD
- Type
- protein
- Length
- 6 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ggvlvn peptide, amyloid forming segment
- UniProt
- P15309
- Ligands
- ZN
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ggvlvn peptide, amyloid forming segment | protein | 6 | 0% helix, 0% strand | P15309 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3PPD · GGVLVN segment from Human Prostatic Acid Phosphatase Residues 260-265, involved in… · the same entry in another collection · chain A against A, TM-score 1.00
- P15309 · AlphaFold monomer V2.0 prediction for prostatic acid phosphatase (P15309) · a predicted model of the same protein · chain A against A, TM-score 0.61
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 P15309
- Elsewhere: RCSB PDB 3PPD · PDBe 3PPD · UniProt P15309
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