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ID of heme Axial ligands on heme Function & structure
3h1h-C-501
sad. +0.17
ruf. -0.22
dom. -0.09
bre. +0.24
HIS chainID: C,
resSeq: 84,
molecule: Cytochrome b
oxidoreductase
oligomeric count: 20
pocket vol.: 422.0 Å3
d(Fe-oop): 0.046 Å
HIS chainID: C, resSeq: 183,

molecule: Cytochrome b

3h1h-C-502
sad. -0.72
ruf. -0.40
dom. +0.05
bre. +0.20
HIS chainID: C,
resSeq: 98,
molecule: Cytochrome b
oxidoreductase
oligomeric count: 20
pocket vol.: 374.0 Å3
d(Fe-oop): 0.016 Å
HIS chainID: C, resSeq: 197,

molecule: Cytochrome b

3h1h-D-501
sad. +0.07
ruf. -0.23
dom. -0.05
bre. +0.30
HIS chainID: D,
resSeq: 41,
molecule: CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL
oxidoreductase
oligomeric count: 20
pocket vol.: 450.0 Å3
d(Fe-oop): 0.019 Å
MET chainID: D, resSeq: 160,

molecule: CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL

3h1h-P-501
sad. +0.37
ruf. -0.21
dom. -0.12
bre. +0.21
HIS chainID: P,
resSeq: 84,
molecule: Cytochrome b
oxidoreductase
oligomeric count: 20
pocket vol.: 437.0 Å3
d(Fe-oop): 0.058 Å
HIS chainID: P, resSeq: 183,

molecule: Cytochrome b

3h1h-P-502
sad. -0.65
ruf. -0.30
dom. +0.15
bre. +0.13
HIS chainID: P,
resSeq: 98,
molecule: Cytochrome b
oxidoreductase
oligomeric count: 20
pocket vol.: 379.0 Å3
d(Fe-oop): 0.017 Å
HIS chainID: P, resSeq: 197,

molecule: Cytochrome b

3h1h-Q-501
sad. +0.08
ruf. -0.15
dom. +0.00
bre. +0.25
HIS chainID: Q,
resSeq: 41,
molecule: CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL
oxidoreductase
oligomeric count: 20
pocket vol.: 488.0 Å3
d(Fe-oop): 0.035 Å
MET chainID: Q, resSeq: 160,

molecule: CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL