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ID of heme Axial ligands on heme Function & structure
3l72-C-501
sad. +0.17
ruf. -0.29
dom. -0.17
bre. +0.11
HIS chainID: C,
resSeq: 84,
molecule: CYTOCHROME B
oxidoreductase
oligomeric count: 20
pocket vol.: 388.0 Å3
d(Fe-oop): 0.031 Å
HIS chainID: C, resSeq: 183,

molecule: CYTOCHROME B

3l72-C-502
sad. -0.80
ruf. -0.29
dom. +0.15
bre. +0.08
HIS chainID: C,
resSeq: 98,
molecule: CYTOCHROME B
oxidoreductase
oligomeric count: 20
pocket vol.: 381.0 Å3
d(Fe-oop): 0.057 Å
HIS chainID: C, resSeq: 197,

molecule: CYTOCHROME B

3l72-D-501
sad. +0.18
ruf. -0.07
dom. -0.10
bre. +0.14
HIS chainID: D,
resSeq: 41,
molecule: MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN
oxidoreductase
oligomeric count: 20
pocket vol.: 452.0 Å3
d(Fe-oop): 0.025 Å
MET chainID: D, resSeq: 160,

molecule: MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN

3l72-P-501
sad. +0.31
ruf. -0.19
dom. -0.22
bre. +0.11
HIS chainID: P,
resSeq: 84,
molecule: CYTOCHROME B
oxidoreductase
oligomeric count: 20
pocket vol.: 400.0 Å3
d(Fe-oop): 0.001 Å
HIS chainID: P, resSeq: 183,

molecule: CYTOCHROME B

3l72-P-502
sad. -0.83
ruf. -0.26
dom. +0.21
bre. +0.07
HIS chainID: P,
resSeq: 98,
molecule: CYTOCHROME B
oxidoreductase
oligomeric count: 20
pocket vol.: 373.0 Å3
d(Fe-oop): 0.010 Å
HIS chainID: P, resSeq: 197,

molecule: CYTOCHROME B

3l72-Q-501
sad. +0.11
ruf. +0.01
dom. -0.10
bre. +0.08
HIS chainID: Q,
resSeq: 41,
molecule: MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN
oxidoreductase
oligomeric count: 20
pocket vol.: 434.0 Å3
d(Fe-oop): 0.027 Å
MET chainID: Q, resSeq: 160,

molecule: MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN