2DC3

Crystal structure of human cytoglobin at 1.68 angstroms resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001666	biological_process	response to hypoxia
A	0004096	molecular_function	catalase activity
A	0004601	molecular_function	peroxidase activity
A	0004784	molecular_function	superoxide dismutase activity
A	0005344	molecular_function	oxygen carrier activity
A	0005506	molecular_function	iron ion binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006979	biological_process	response to oxidative stress
A	0010764	biological_process	negative regulation of fibroblast migration
A	0015671	biological_process	oxygen transport
A	0016209	molecular_function	antioxidant activity
A	0016491	molecular_function	oxidoreductase activity
A	0016607	cellular_component	nuclear speck
A	0019395	biological_process	fatty acid oxidation
A	0019430	biological_process	removal of superoxide radicals
A	0019825	molecular_function	oxygen binding
A	0020037	molecular_function	heme binding
A	0032966	biological_process	negative regulation of collagen biosynthetic process
A	0043005	cellular_component	neuron projection
A	0043025	cellular_component	neuronal cell body
A	0046209	biological_process	nitric oxide metabolic process
A	0046210	biological_process	nitric oxide catabolic process
A	0046872	molecular_function	metal ion binding
A	0047888	molecular_function	fatty acid peroxidase activity
A	0070025	molecular_function	carbon monoxide binding
A	0098809	molecular_function	nitrite reductase activity
A	0141118	molecular_function	nitric oxide dioxygenase activity, heme protein as donor
A	2000490	biological_process	negative regulation of hepatic stellate cell activation
B	0001666	biological_process	response to hypoxia
B	0004096	molecular_function	catalase activity
B	0004601	molecular_function	peroxidase activity
B	0004784	molecular_function	superoxide dismutase activity
B	0005344	molecular_function	oxygen carrier activity
B	0005506	molecular_function	iron ion binding
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006979	biological_process	response to oxidative stress
B	0010764	biological_process	negative regulation of fibroblast migration
B	0015671	biological_process	oxygen transport
B	0016209	molecular_function	antioxidant activity
B	0016491	molecular_function	oxidoreductase activity
B	0016607	cellular_component	nuclear speck
B	0019395	biological_process	fatty acid oxidation
B	0019430	biological_process	removal of superoxide radicals
B	0019825	molecular_function	oxygen binding
B	0020037	molecular_function	heme binding
B	0032966	biological_process	negative regulation of collagen biosynthetic process
B	0043005	cellular_component	neuron projection
B	0043025	cellular_component	neuronal cell body
B	0046209	biological_process	nitric oxide metabolic process
B	0046210	biological_process	nitric oxide catabolic process
B	0046872	molecular_function	metal ion binding
B	0047888	molecular_function	fatty acid peroxidase activity
B	0070025	molecular_function	carbon monoxide binding
B	0098809	molecular_function	nitrite reductase activity
B	0141118	molecular_function	nitric oxide dioxygenase activity, heme protein as donor
B	2000490	biological_process	negative regulation of hepatic stellate cell activation

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEM A 191

Chain	Residue
A	ALA56
A	VAL119
A	TYR123
A	PHE124
A	HOH1212
A	HOH1237
A	HOH1314
A	HOH1331
A	HOH1340
A	HOH1348
A	TYR59
A	PHE60
A	GLN77
A	HIS81
A	ARG84
A	VAL85
A	HIS113
A	HIS117

---

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEM B 191

Chain	Residue
B	ALA56
B	TYR59
B	PHE60
B	GLN77
B	HIS81
B	VAL85
B	HIS113
B	HIS117
B	VAL119
B	PHE124
B	LEU127
B	HOH206
B	HOH219
B	HOH223
B	HOH226
B	HOH286
B	HOH296

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ACY A 1200

Chain	Residue
A	TYR35
A	CYS83
A	GLY87
A	HOH1211
A	HOH1292
B	TYR35
B	CYS83
B	GLY87

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	298
Details	Domain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"description":"distal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15044115","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15095869","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15165856","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16699195","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1URV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1URY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1UT0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1UX9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1V5H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2DC3","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"description":"proximal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15044115","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15095869","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15165856","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16699195","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1UMO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1URV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1URY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1UT0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1UX9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1V5H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2DC3","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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