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Crystal structure of ferredoxin: thioredoxin reductase and thioredoxin M2 complex
Analyse Crystal structure of ferredoxin: thioredoxin reductase and thioredoxin M2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7C3F
- Type
- protein
- Length
- 2,328 residues
- Chains
- 23
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic; Ferredoxin-thioredoxin…
- EC
- 1.8.7.2
- UniProt
- Q9SJ89, Q8LBP6, Q9SEU8
- Ligands
- SF4, NA
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 10 distinct chains · 34% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, J | Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic (EC 1.8.7.2) | protein | 113 | 50% helix, 6% strand | Q9SJ89 |
| B, H, K, N, Q | Ferredoxin-thioredoxin reductase variable chain, chloroplastic | protein | 88 | 13% helix, 45% strand | Q8LBP6 |
| C, F, L, O, R, U | Thioredoxin M2, chloroplastic | protein | 107 | 34% helix, 26% strand | Q9SEU8 |
| D, G, M, S | Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic (EC 1.8.7.2) | protein | 114 | 49% helix, 6% strand | Q9SJ89 |
| E | Ferredoxin-thioredoxin reductase variable chain, chloroplastic | protein | 89 | 13% helix, 45% strand | Q8LBP6 |
| I | Thioredoxin M2, chloroplastic | protein | 106 | 33% helix, 26% strand | Q9SEU8 |
| P | Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic (EC 1.8.7.2) | protein | 113 | 50% helix, 6% strand | Q9SJ89 |
| T | Ferredoxin-thioredoxin reductase variable chain, chloroplastic | protein | 87 | 13% helix, 37% strand | Q8LBP6 |
| W | Thioredoxin M2, chloroplastic | protein | 98 | 35% helix, 22% strand | Q9SEU8 |
| V | Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic (EC 1.8.7.2) | protein | 71 | 34% helix, 6% strand | Q9SJ89 |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · 7 copies · chains A, D, G, J, M, P, S
- NA · Sodium ion · metal · 10 copies · chains A, C, D, F, E, G, J, L, O, M, P, Q, R
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1008 | 0.79 | 0.81 | 94 | empty |
| 2 | 673 | 0.74 | 0.80 | 97 | empty |
| 3 | 919 | 0.72 | 0.76 | 104 | empty |
| 4 | 666 | 0.70 | 0.78 | 79 | empty |
| 5 | 590 | 0.68 | 0.77 | 68 | empty |
Interfaces
50 interfaces between chains.
- P–R · 874 Ų buried · 7 hydrogen bonds · protein-protein
- S–U · 855 Ų buried · 6 hydrogen bonds · protein-protein
- D–F · 855 Ų buried · 6 hydrogen bonds · protein-protein
- M–O · 836 Ų buried · 9 hydrogen bonds · protein-protein
- G–I · 835 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 7C3F · Crystal structure of ferredoxin: thioredoxin reductase and thioredoxin m2 complex · the same entry in another collection · chain J against J, 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 Q9SJ89
- Every structure of UniProt Q8LBP6
- Every structure of UniProt Q9SEU8
- Elsewhere: RCSB PDB 7C3F · PDBe 7C3F · UniProt Q9SJ89 · UniProt Q8LBP6 · UniProt Q9SEU8
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