MolNFT v1 · #25892 · protein
The mechanism of the schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates
1W8S: “The mechanism of the schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction…”. X-ray diffraction. MolNFT v1 #25892 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1W8S
- Type
- protein
- Length
- 2,502 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P58315
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, F, G, H, I, J | — | protein | 250 | — | P58315 |
| E | — | protein | 252 | — | P58315 |
Compared structures
- 1W8S · The mechanism of the Schiff Base Forming Fructose-1,6-bisphosphate Aldolase: Structural… · the same entry in another collection · chain J against J, TM-score 1.00
- P58315 · AlphaFold monomer V2.0 prediction for fructose-bisphosphate aldolase class 1 (P58315) · a predicted model of the same protein · chain E 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
- Every structure of UniProt P58315
- Elsewhere: RCSB PDB 1W8S · PDBe 1W8S · UniProt P58315
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