Research workbench
Marsupenaeus japonicus ferritin mutant (T158H)
Analyse Marsupenaeus japonicus ferritin mutant (T158H) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LRU
- Type
- protein
- Length
- 169 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferritin
- EC
- 1.16.3.1
- UniProt
- T2B7E1
- Ligands
- NI, FE
Structure
x-ray diffraction · 1 distinct chain · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferritin (EC 1.16.3.1) | protein | 169 | 74% helix, 0% strand | T2B7E1 |
Ligands and binding sites
- NI · Nickel (II) ion · metal · 2 copies · chains A
- FE · Fe (III) ion · metal · chains A
- IMD · Imidazole · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6LRU · Marsupenaeus japonicus ferritin mutant (T158H) · 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 6LRU · PDBe 6LRU · UniProt T2B7E1
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