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Protein data
function: oxidoreductaseexperiment: X-RAY DIFFRACTION
resolution: 2.95 Å
axial ligand #1: MET
chainID: G,resSeq: 52,
Coordination distance[Å]: 2.241
molecule: BACTERIOFERRITIN
Organism: ESCHERICHIA COLI
axial ligand #2: MET
chainID: H,resSeq: 52,
Coordination distance[Å]: 2.161
molecule: BACTERIOFERRITIN
Organism: ESCHERICHIA COLI
List of other hemes in pdb:3e1o
ID of heme | Distortion | Axial ligands on heme | Function & structure | |
---|---|---|---|---|
3e1o-A-200 |
sad. -0.27 ruf. +0.20 dom. +0.16 bre. -0.41 |
MET | chainID: A, resSeq: 52, molecule: BACTERIOFERRITIN |
oxidoreductase oligomeric count: 24 pocket vol.: 521.0 Å3 d(Fe-oop): 0.032 Å |
MET | chainID: B, resSeq: 52, molecule: BACTERIOFERRITIN |
|||
3e1o-D-200 |
sad. -0.28 ruf. +0.20 dom. +0.16 bre. -0.42 |
MET | chainID: C, resSeq: 52, molecule: BACTERIOFERRITIN |
oxidoreductase oligomeric count: 24 pocket vol.: 533.0 Å3 d(Fe-oop): 0.035 Å |
MET | chainID: D, resSeq: 52, molecule: BACTERIOFERRITIN |
|||
3e1o-E-200 |
sad. -0.28 ruf. +0.20 dom. +0.16 bre. -0.41 |
MET | chainID: E, resSeq: 52, molecule: BACTERIOFERRITIN |
oxidoreductase oligomeric count: 24 pocket vol.: 521.0 Å3 d(Fe-oop): 0.031 Å |
MET | chainID: F, resSeq: 52, molecule: BACTERIOFERRITIN |
|||
3e1o-I-200 |
sad. -0.28 ruf. +0.20 dom. +0.16 bre. -0.42 |
MET | chainID: I, resSeq: 52, molecule: BACTERIOFERRITIN |
oxidoreductase oligomeric count: 24 pocket vol.: 542.0 Å3 d(Fe-oop): 0.030 Å |
MET | chainID: J, resSeq: 52, molecule: BACTERIOFERRITIN |
|||
3e1o-K-200 |
sad. -0.28 ruf. +0.20 dom. +0.16 bre. -0.42 |
MET | chainID: K, resSeq: 52, molecule: BACTERIOFERRITIN |
oxidoreductase oligomeric count: 24 pocket vol.: 543.0 Å3 d(Fe-oop): 0.031 Å |
MET | chainID: L, resSeq: 52, molecule: BACTERIOFERRITIN |