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ID of heme Axial ligands on heme Function & structure
3h1i-C-501
sad. -0.28
ruf. -0.10
dom. -0.04
bre. +0.27
HIS chainID: C,
resSeq: 84,
molecule: Cytochrome b
oxidoreductase
oligomeric count: 20
pocket vol.: 386.0 Å3
d(Fe-oop): 0.021 Å
HIS chainID: C, resSeq: 183,

molecule: Cytochrome b

3h1i-C-502
sad. -0.71
ruf. -0.18
dom. +0.09
bre. +0.21
HIS chainID: C,
resSeq: 98,
molecule: Cytochrome b
oxidoreductase
oligomeric count: 20
pocket vol.: 379.0 Å3
d(Fe-oop): 0.004 Å
HIS chainID: C, resSeq: 197,

molecule: Cytochrome b

3h1i-D-501
sad. +0.18
ruf. -0.01
dom. -0.01
bre. +0.13
HIS chainID: D,
resSeq: 41,
molecule: CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL
oxidoreductase
oligomeric count: 20
pocket vol.: 418.0 Å3
d(Fe-oop): 0.022 Å
MET chainID: D, resSeq: 160,

molecule: CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL

3h1i-P-501
sad. +0.03
ruf. -0.08
dom. -0.13
bre. +0.24
HIS chainID: P,
resSeq: 84,
molecule: Cytochrome b
oxidoreductase
oligomeric count: 20
pocket vol.: 387.0 Å3
d(Fe-oop): 0.006 Å
HIS chainID: P, resSeq: 183,

molecule: Cytochrome b

3h1i-P-502
sad. -0.66
ruf. -0.04
dom. +0.13
bre. +0.18
HIS chainID: P,
resSeq: 98,
molecule: Cytochrome b
oxidoreductase
oligomeric count: 20
pocket vol.: 364.0 Å3
d(Fe-oop): 0.004 Å
HIS chainID: P, resSeq: 197,

molecule: Cytochrome b

3h1i-Q-501
sad. +0.13
ruf. +0.08
dom. -0.05
bre. +0.17
HIS chainID: Q,
resSeq: 41,
molecule: CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL
oxidoreductase
oligomeric count: 20
pocket vol.: 433.0 Å3
d(Fe-oop): 0.007 Å
MET chainID: Q, resSeq: 160,

molecule: CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL