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Crystal structure of fructose-bisphosphate aldolase from plasmodium falciparum in complex with trap-tail determined at 2.4 ångström resolution
Analyse Crystal structure of fructose-bisphosphate aldolase from plasmodium falciparum… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PC4
- Type
- protein
- Length
- 1,429 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P14223, P90573
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 359 | — | P14223 |
| B, D | — | protein | 351 | — | P14223 |
| C | — | protein | 365 | — | P14223 |
| H | — | protein | 3 | — | P90573 |
Compared structures
- 2PC4 · Crystal structure of fructose-bisphosphate aldolase from Plasmodium falciparum in complex… · the same entry in another collection · chain H against H, TM-score 1.00
- P14223 · AlphaFold monomer V2.0 prediction for fructose-bisphosphate aldolase (P14223) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 P14223
- Every structure of UniProt P90573
- Elsewhere: RCSB PDB 2PC4 · PDBe 2PC4 · UniProt P14223 · UniProt P90573
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