Research workbench
Structure of ceruloplasmin-myeloperoxidase complex
Analyse Structure of ceruloplasmin-myeloperoxidase complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EJX
- Type
- protein
- Length
- 1,604 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00450, P05164
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1034 | — | P00450 |
| B | — | protein | 104 | — | P05164 |
| D | — | protein | 466 | — | P05164 |
Compared structures
- 4EJX · Structure of ceruloplasmin-myeloperoxidase complex · the same entry in another collection · chain A against A, TM-score 1.00
- P00450 · AlphaFold monomer V2.0 prediction for ceruloplasmin (P00450) · a predicted model of the same protein · chain A against A, TM-score 0.99
- P05164 · AlphaFold monomer V2.0 prediction for myeloperoxidase (P05164) · a predicted model of the same protein · chain D 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 P00450
- Every structure of UniProt P05164
- Elsewhere: RCSB PDB 4EJX · PDBe 4EJX · UniProt P00450 · UniProt P05164
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