Browser
ID of heme | Axial ligands on heme | Function & structure | ||
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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 |
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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 |
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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 |
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2htn-G-200 |
sad. -0.21 ruf. +0.17 dom. +0.15 bre. -0.28 |
MET | chainID: G, resSeq: 52, molecule: Bacterioferritin |
oxidoreductase oligomeric count: 24 pocket vol.: 626.0 Å3 d(Fe-oop): 0.016 Å |
MET | chainID: H, resSeq: 52, molecule: Bacterioferritin |