Research workbench
Vipoxin complex
Analyse Vipoxin complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AOK
- Type
- protein
- Length
- 244 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P04084, P14420
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 122 | — | P04084 |
| B | — | protein | 122 | — | P14420 |
Compared structures
- 1AOK · Vipoxin complex · the same entry in another collection · chain A against A, TM-score 1.00
- P04084 · AlphaFold monomer V2.0 prediction for acidic phospholipase A2 homolog vipoxin a chain… · a predicted model of the same protein · chain A against A, TM-score 0.98
- P14420 · AlphaFold monomer V2.0 prediction for basic phospholipase A2 vipoxin B chain (P14420) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 P04084
- Every structure of UniProt P14420
- Elsewhere: RCSB PDB 1AOK · PDBe 1AOK · UniProt P04084 · UniProt P14420
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