MolNFT v1 · #176557 · protein
Marsupenaeus japonicus ferritin mutant-D132R
7DQO: “Marsupenaeus japonicus ferritin mutant-D132R”. X-ray diffraction, 1 ligand (FE), 20 pockets (best druggability 0.83). MolNFT v1 #176557 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7DQO
- Type
- protein
- Length
- 2,028 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferritin
- EC
- 1.16.3.1
- UniProt
- T2B7E1
- Ligands
- FE
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 74% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | Ferritin (EC 1.16.3.1) | protein | 169 | 74% helix, 1% strand | T2B7E1 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 12 copies · chains A, B, C, D, E, F, G, H, I, J, K, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 990 | 0.83 | 0.84 | 106 | empty |
| 2 | 643 | 0.79 | 0.84 | 75 | empty |
| 3 | 120 | 0.77 | 0.95 | 21 | empty |
| 4 | 79 | 0.77 | 0.98 | 14 | empty |
| 5 | 94 | 0.77 | 0.97 | 16 | empty |
Interfaces
20 interfaces between chains.
- B–D · 1489 Ų buried · 27 hydrogen bonds · protein-protein
- F–H · 1487 Ų buried · 31 hydrogen bonds · protein-protein
- J–L · 1463 Ų buried · 31 hydrogen bonds · protein-protein
- I–K · 1461 Ų buried · 29 hydrogen bonds · protein-protein
- A–C · 1458 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 7DQO · Marsupenaeus japonicus ferritin mutant-D132R · the same entry in another collection · chain A 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 T2B7E1
- Elsewhere: RCSB PDB 7DQO · PDBe 7DQO · UniProt T2B7E1
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