5ZLG

Human duodenal cytochrome b (Dcytb) in zinc ion and ascorbate bound form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005765	cellular_component	lysosomal membrane
A	0005886	cellular_component	plasma membrane
A	0006879	biological_process	intracellular iron ion homeostasis
A	0010039	biological_process	response to iron ion
A	0016020	cellular_component	membrane
A	0016324	cellular_component	apical plasma membrane
A	0016491	molecular_function	oxidoreductase activity
A	0016722	molecular_function	oxidoreductase activity, acting on metal ions
A	0031526	cellular_component	brush border membrane
A	0033215	biological_process	reductive iron assimilation
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0055085	biological_process	transmembrane transport
A	0060586	biological_process	multicellular organismal-level iron ion homeostasis
A	0070062	cellular_component	extracellular exosome
A	0140571	molecular_function	transmembrane ascorbate ferrireductase activity
A	0140575	molecular_function	transmembrane monodehydroascorbate reductase activity
A	0140576	biological_process	ascorbate homeostasis

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	83
Details	TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:30272000

Chain	Residue	Details
A	MET1-TRP7
A	ARG70-SER78
A	PRO145-LEU151
A	GLN223-MET286

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site_id	SWS_FT_FI2
Number of Residues	24
Details	TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:30272000, ECO:0007744|PDB:5ZLE, ECO:0007744|PDB:5ZLG

Chain	Residue	Details
A	ARG8-LEU32

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site_id	SWS_FT_FI3
Number of Residues	43
Details	TOPO_DOM: Extracellular => ECO:0000305|PubMed:30272000

Chain	Residue	Details
A	HIS33-PHE47
A	GLU106-SER118
A	GLU180-GLU197

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site_id	SWS_FT_FI4
Number of Residues	21
Details	TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:30272000, ECO:0007744|PDB:5ZLE, ECO:0007744|PDB:5ZLG

Chain	Residue	Details
A	ASN48-TYR69

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site_id	SWS_FT_FI5
Number of Residues	26
Details	TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:30272000, ECO:0007744|PDB:5ZLE, ECO:0007744|PDB:5ZLG

Chain	Residue	Details
A	LYS79-PHE105

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site_id	SWS_FT_FI6
Number of Residues	25
Details	TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:30272000, ECO:0007744|PDB:5ZLE, ECO:0007744|PDB:5ZLG

Chain	Residue	Details
A	LEU119-LEU144

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site_id	SWS_FT_FI7
Number of Residues	27
Details	TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:30272000, ECO:0007744|PDB:5ZLE, ECO:0007744|PDB:5ZLG

Chain	Residue	Details
A	ARG152-THR179

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site_id	SWS_FT_FI8
Number of Residues	24
Details	TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:30272000, ECO:0007744|PDB:5ZLE, ECO:0007744|PDB:5ZLG

Chain	Residue	Details
A	GLY198-PRO222

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site_id	SWS_FT_FI9
Number of Residues	4
Details	BINDING: axial binding residue => ECO:0000269|PubMed:30272000, ECO:0007744|PDB:5ZLE, ECO:0007744|PDB:5ZLG

Chain	Residue	Details
A	HIS50
A	HIS86
A	HIS120
A	HIS159

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site_id	SWS_FT_FI10
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:30272000, ECO:0007744|PDB:5ZLE, ECO:0007744|PDB:5ZLG

Chain	Residue	Details
A	ARG70
A	LYS79
A	LYS83
A	HIS108
A	ASN115
A	ARG152
A	GLU180
A	LYS225

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site_id	SWS_FT_FI11
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER232

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site_id	SWS_FT_FI12
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	THR285

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