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Protein data
function: oxidoreductaseexperiment: X-RAY DIFFRACTION
resolution: 2.4 Å
axial ligand #1: MET
chainID: I,resSeq: 52,
Coordination distance[Å]: 2.223
molecule: BACTERIOFERRITIN
Organism: ESCHERICHIA COLI
axial ligand #2: MET
chainID: J,resSeq: 52,
Coordination distance[Å]: 2.117
molecule: BACTERIOFERRITIN
Organism: ESCHERICHIA COLI
List of other hemes in pdb:3e1p
ID of heme | Distortion | Axial ligands on heme | Function & structure | |
---|---|---|---|---|
3e1p-A-200 |
sad. -0.33 ruf. +0.15 dom. +0.13 bre. -0.40 |
MET | chainID: A, resSeq: 52, molecule: BACTERIOFERRITIN |
oxidoreductase oligomeric count: 24 pocket vol.: 507.0 Å3 d(Fe-oop): 0.040 Å |
MET | chainID: B, resSeq: 52, molecule: BACTERIOFERRITIN |
|||
3e1p-C-200 |
sad. -0.32 ruf. +0.15 dom. +0.13 bre. -0.40 |
MET | chainID: C, resSeq: 52, molecule: BACTERIOFERRITIN |
oxidoreductase oligomeric count: 24 pocket vol.: 494.0 Å3 d(Fe-oop): 0.041 Å |
MET | chainID: D, resSeq: 52, molecule: BACTERIOFERRITIN |
|||
3e1p-F-200 |
sad. -0.33 ruf. +0.15 dom. +0.13 bre. -0.40 |
MET | chainID: E, resSeq: 52, molecule: BACTERIOFERRITIN |
oxidoreductase oligomeric count: 24 pocket vol.: 491.0 Å3 d(Fe-oop): 0.041 Å |
MET | chainID: F, resSeq: 52, molecule: BACTERIOFERRITIN |
|||
3e1p-H-200 |
sad. -0.33 ruf. +0.15 dom. +0.13 bre. -0.40 |
MET | chainID: G, resSeq: 52, molecule: BACTERIOFERRITIN |
oxidoreductase oligomeric count: 24 pocket vol.: 513.0 Å3 d(Fe-oop): 0.039 Å |
MET | chainID: H, resSeq: 52, molecule: BACTERIOFERRITIN |
|||
3e1p-K-200 |
sad. -0.33 ruf. +0.15 dom. +0.13 bre. -0.40 |
MET | chainID: K, resSeq: 52, molecule: BACTERIOFERRITIN |
oxidoreductase oligomeric count: 24 pocket vol.: 516.0 Å3 d(Fe-oop): 0.040 Å |
MET | chainID: L, resSeq: 52, molecule: BACTERIOFERRITIN |