Research workbench
Crystal structure of chlamydomonas reinhardtii chloroplastic fructose bisphosphate aldolase
Analyse Crystal structure of chlamydomonas reinhardtii chloroplastic fructose… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7B2N
- Type
- protein
- Length
- 2,649 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-bisphosphate aldolase 1, chloroplastic
- EC
- 4.1.2.13
- UniProt
- Q42690
- Ligands
- SO4, CL
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 8 distinct chains · 48% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructose-bisphosphate aldolase 1, chloroplastic (EC 4.1.2.13) | protein | 332 | 47% helix, 16% strand | Q42690 |
| B | Fructose-bisphosphate aldolase 1, chloroplastic (EC 4.1.2.13) | protein | 332 | 48% helix, 16% strand | Q42690 |
| C | Fructose-bisphosphate aldolase 1, chloroplastic (EC 4.1.2.13) | protein | 332 | 48% helix, 17% strand | Q42690 |
| D | Fructose-bisphosphate aldolase 1, chloroplastic (EC 4.1.2.13) | protein | 329 | 49% helix, 16% strand | Q42690 |
| E | Fructose-bisphosphate aldolase 1, chloroplastic (EC 4.1.2.13) | protein | 333 | 47% helix, 16% strand | Q42690 |
| F | Fructose-bisphosphate aldolase 1, chloroplastic (EC 4.1.2.13) | protein | 331 | 48% helix, 16% strand | Q42690 |
| G | Fructose-bisphosphate aldolase 1, chloroplastic (EC 4.1.2.13) | protein | 330 | 49% helix, 16% strand | Q42690 |
| H | Fructose-bisphosphate aldolase 1, chloroplastic (EC 4.1.2.13) | protein | 330 | 48% helix, 17% strand | Q42690 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 29 copies · chains A, H, B, D, C, G, E, F
- CL · Chloride ion · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 864 | 0.85 | 0.87 | 94 | SO4 |
| 2 | 916 | 0.85 | 0.86 | 103 | SO4 |
| 3 | 978 | 0.82 | 0.83 | 101 | empty |
| 4 | 70 | 0.76 | 0.99 | 18 | empty |
| 5 | 70 | 0.75 | 0.99 | 18 | empty |
Interfaces
15 interfaces between chains.
- C–E · 1164 Ų buried · 27 hydrogen bonds · protein-protein
- F–G · 1159 Ų buried · 25 hydrogen bonds · protein-protein
- B–H · 1153 Ų buried · 27 hydrogen bonds · protein-protein
- A–D · 1149 Ų buried · 25 hydrogen bonds · protein-protein
- A–B · 793 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 7B2N · Crystal structure of Chlamydomonas reinhardtii chloroplastic Fructose bisphosphate… · the same entry in another collection · chain H against H, TM-score 1.00
- Q42690 · AlphaFold monomer V2.0 prediction for fructose-bisphosphate aldolase 1, chloroplastic… · a predicted model of the same protein · chain G 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 Q42690
- Elsewhere: RCSB PDB 7B2N · PDBe 7B2N · UniProt Q42690
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