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Protein data
function: oxidoreductaseexperiment: X-RAY DIFFRACTION
resolution: 2.5 Å
axial ligand #1: MET
chainID: E,resSeq: 52,
Coordination distance[Å]: 2.049
molecule: BACTERIOFERRITIN
Organism: ESCHERICHIA COLI
axial ligand #2: MET
chainID: F,resSeq: 52,
Coordination distance[Å]: 2.068
molecule: BACTERIOFERRITIN
Organism: ESCHERICHIA COLI
List of other hemes in pdb:3e1l
| ID of heme | Distortion | Axial ligands on heme | Function & structure | |
|---|---|---|---|---|
3e1l-A-200 |
sad. -0.26 ruf. +0.13 dom. +0.09 bre. -0.42 |
MET | chainID: A, resSeq: 52, molecule: BACTERIOFERRITIN |
oxidoreductase oligomeric count: 24 pocket vol.: 498.0 Å3 d(Fe-oop): 0.001 Å |
| MET | chainID: B, resSeq: 52, molecule: BACTERIOFERRITIN |
|||
3e1l-C-200 |
sad. -0.28 ruf. +0.13 dom. +0.07 bre. -0.43 |
MET | chainID: C, resSeq: 52, molecule: BACTERIOFERRITIN |
oxidoreductase oligomeric count: 24 pocket vol.: 496.0 Å3 d(Fe-oop): 0.038 Å |
| MET | chainID: D, resSeq: 52, molecule: BACTERIOFERRITIN |
|||
3e1l-G-200 |
sad. -0.30 ruf. +0.09 dom. +0.13 bre. -0.42 |
MET | chainID: G, resSeq: 52, molecule: BACTERIOFERRITIN |
oxidoreductase oligomeric count: 24 pocket vol.: 506.0 Å3 d(Fe-oop): 0.016 Å |
| MET | chainID: H, resSeq: 52, molecule: BACTERIOFERRITIN |
|||
3e1l-I-200 |
sad. -0.32 ruf. +0.06 dom. +0.09 bre. -0.42 |
MET | chainID: I, resSeq: 52, molecule: BACTERIOFERRITIN |
oxidoreductase oligomeric count: 24 pocket vol.: 495.0 Å3 d(Fe-oop): 0.005 Å |
| MET | chainID: J, resSeq: 52, molecule: BACTERIOFERRITIN |
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