Research workbench
Crystal structure of E. COLI bacterioferritin (bfr) in which the ferroxidase centre is inhibited with ZN(II) and high occupancy iron is bound within the cavity.
Analyse Crystal structure of E. COLI bacterioferritin (bfr) in which the ferroxidase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3E1P
- Type
- protein
- Length
- 1,896 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0ABD3
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | — | protein | 158 | — | P0ABD3 |
Compared structures
- 3E1P · Crystal structure of E. coli Bacterioferritin (BFR) in which the Ferroxidase centre is… · the same entry in another collection · chain L against L, 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 P0ABD3
- Elsewhere: RCSB PDB 3E1P · PDBe 3E1P · UniProt P0ABD3
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