MolNFT v1 · #75301 · protein
Crystal structure of a putative fructose-1,6-biphosphate aldolase from coccidioides immitis solved by combined sad mr
3PM6 · Putative fructose-bisphosphate aldolase: “Crystal structure of a putative fructose-1,6-biphosphate aldolase from coccidioides immitis solved by…”. X-ray diffraction, 2 ligands (ZN, IOD), 4 pockets (best druggability 0.37). MolNFT v1…
- PDB
- 3PM6
- Type
- protein
- Length
- 551 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative fructose-bisphosphate aldolase
- EC
- 4.1.2.13
- UniProt
- P0CJ44
- Ligands
- ZN, IOD
- Pockets
- 4 · best druggability 0.37
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative fructose-bisphosphate aldolase (EC 4.1.2.13) | protein | 287 | 47% helix, 15% strand | P0CJ44 |
| B | Putative fructose-bisphosphate aldolase (EC 4.1.2.13) | protein | 264 | 51% helix, 14% strand | P0CJ44 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 97 | 0.37 | 0.75 | 23 | IOD |
| 2 | 81 | 0.34 | 0.75 | 14 | empty |
| 3 | 67 | 0.32 | 0.75 | 15 | empty |
| 4 | 52 | 0.30 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1384 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 3PM6 · Crystal structure of a putative fructose-1,6-biphosphate aldolase from Coccidioides… · the same entry in another collection · chain A against A, TM-score 1.00
- P0CJ44 · AlphaFold monomer V2.0 prediction for putative fructose-bisphosphate aldolase (P0CJ44) · 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 P0CJ44
- Elsewhere: RCSB PDB 3PM6 · PDBe 3PM6 · UniProt P0CJ44
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