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ID of heme Axial ligands on heme Function & structure
3h1k-C-501
sad. +0.25
ruf. -0.46
dom. -0.25
bre. +0.30
HIS chainID: C,
resSeq: 84,
molecule: Cytochrome b
oxidoreductase
oligomeric count: 20
pocket vol.: 386.0 Å3
d(Fe-oop): 0.030 Å
HIS chainID: C, resSeq: 183,

molecule: Cytochrome b

3h1k-C-502
sad. -0.60
ruf. -0.16
dom. +0.20
bre. +0.29
HIS chainID: C,
resSeq: 98,
molecule: Cytochrome b
oxidoreductase
oligomeric count: 20
pocket vol.: 360.0 Å3
d(Fe-oop): 0.007 Å
HIS chainID: C, resSeq: 197,

molecule: Cytochrome b

3h1k-D-501
sad. +0.31
ruf. -0.03
dom. -0.09
bre. +0.31
HIS chainID: D,
resSeq: 41,
molecule: MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN
oxidoreductase
oligomeric count: 20
pocket vol.: 426.0 Å3
d(Fe-oop): 0.040 Å
MET chainID: D, resSeq: 160,

molecule: MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN

3h1k-P-501
sad. +0.32
ruf. -0.37
dom. -0.29
bre. +0.22
HIS chainID: P,
resSeq: 84,
molecule: Cytochrome b
oxidoreductase
oligomeric count: 20
pocket vol.: 402.0 Å3
d(Fe-oop): 0.024 Å
HIS chainID: P, resSeq: 183,

molecule: Cytochrome b

3h1k-P-502
sad. -0.68
ruf. -0.08
dom. +0.30
bre. +0.21
HIS chainID: P,
resSeq: 98,
molecule: Cytochrome b
oxidoreductase
oligomeric count: 20
pocket vol.: 348.0 Å3
d(Fe-oop): 0.001 Å
HIS chainID: P, resSeq: 197,

molecule: Cytochrome b

3h1k-Q-501
sad. +0.24
ruf. -0.02
dom. -0.13
bre. +0.25
HIS chainID: Q,
resSeq: 41,
molecule: MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN
oxidoreductase
oligomeric count: 20
pocket vol.: 454.0 Å3
d(Fe-oop): 0.025 Å
MET chainID: Q, resSeq: 160,

molecule: MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN