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ID of heme Axial ligands on heme Function & structure
3h1j-C-501
sad. +0.18
ruf. -0.23
dom. -0.17
bre. +0.11
HIS chainID: C,
resSeq: 84,
molecule: Cytochrome b
oxidoreductase
oligomeric count: 20
pocket vol.: 383.0 Å3
d(Fe-oop): 0.000 Å
HIS chainID: C, resSeq: 183,

molecule: Cytochrome b

3h1j-C-502
sad. -0.62
ruf. -0.22
dom. +0.28
bre. +0.01
HIS chainID: C,
resSeq: 98,
molecule: Cytochrome b
oxidoreductase
oligomeric count: 20
pocket vol.: 332.0 Å3
d(Fe-oop): 0.044 Å
HIS chainID: C, resSeq: 197,

molecule: Cytochrome b

3h1j-D-501
sad. +0.10
ruf. -0.45
dom. -0.13
bre. +0.04
HIS chainID: D,
resSeq: 41,
molecule: MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN
oxidoreductase
oligomeric count: 20
pocket vol.: 419.0 Å3
d(Fe-oop): 0.028 Å
MET chainID: D, resSeq: 160,

molecule: MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN

3h1j-P-501
sad. +0.31
ruf. -0.04
dom. -0.15
bre. +0.09
HIS chainID: P,
resSeq: 84,
molecule: Cytochrome b
oxidoreductase
oligomeric count: 20
pocket vol.: 378.0 Å3
d(Fe-oop): 0.032 Å
HIS chainID: P, resSeq: 183,

molecule: Cytochrome b

3h1j-P-502
sad. -0.67
ruf. -0.19
dom. +0.29
bre. +0.06
HIS chainID: P,
resSeq: 98,
molecule: Cytochrome b
oxidoreductase
oligomeric count: 20
pocket vol.: 353.0 Å3
d(Fe-oop): 0.033 Å
HIS chainID: P, resSeq: 197,

molecule: Cytochrome b

3h1j-Q-501
sad. +0.01
ruf. -0.30
dom. -0.13
bre. +0.03
HIS chainID: Q,
resSeq: 41,
molecule: MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN
oxidoreductase
oligomeric count: 20
pocket vol.: 441.0 Å3
d(Fe-oop): 0.007 Å
MET chainID: Q, resSeq: 160,

molecule: MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN