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Protein data
function: oxidoreductaseexperiment: X-RAY DIFFRACTION
resolution: 2.5 Å
origomeric count: 24
axial ligand #1: MET
chainID: G,resSeq: 52,
Coordination distance[Å]: 2.328
molecule: Bacterioferritin
EC number: 1.16.3.1
Organism: Escherichia coli
axial ligand #2: MET
chainID: H,resSeq: 52,
Coordination distance[Å]: 2.499
molecule: Bacterioferritin
EC number: 1.16.3.1
Organism: Escherichia coli
List of other hemes in pdb:2htn
ID of heme | Distortion | Axial ligands on heme | Function & structure | |
---|---|---|---|---|
2htn-A-200![]() |
sad. -0.33 ruf. +0.14 dom. +0.11 bre. -0.33 |
MET | chainID: A, resSeq: 52, molecule: Bacterioferritin |
oxidoreductase oligomeric count: 24 pocket vol.: 566.0 Å3 d(Fe-oop): 0.005 Å |
MET | chainID: B, resSeq: 52, molecule: Bacterioferritin |
|||
2htn-C-200![]() |
sad. -0.22 ruf. +0.05 dom. +0.20 bre. -0.27 |
MET | chainID: C, resSeq: 52, molecule: Bacterioferritin |
oxidoreductase oligomeric count: 24 pocket vol.: 610.0 Å3 d(Fe-oop): 0.003 Å |
MET | chainID: D, resSeq: 52, molecule: Bacterioferritin |
|||
2htn-E-200![]() |
sad. -0.24 ruf. +0.06 dom. +0.18 bre. -0.33 |
MET | chainID: E, resSeq: 52, molecule: Bacterioferritin |
oxidoreductase oligomeric count: 24 pocket vol.: 612.0 Å3 d(Fe-oop): 0.021 Å |
MET | chainID: F, resSeq: 52, molecule: Bacterioferritin |