6I40

Crystal structure of murine neuroglobin bound to CO at 15K under illumination using optical fiber

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001666	biological_process	response to hypoxia
A	0005092	molecular_function	GDP-dissociation inhibitor activity
A	0005344	molecular_function	oxygen carrier activity
A	0005515	molecular_function	protein binding
A	0005759	cellular_component	mitochondrial matrix
A	0005829	cellular_component	cytosol
A	0015671	biological_process	oxygen transport
A	0016491	molecular_function	oxidoreductase activity
A	0019825	molecular_function	oxygen binding
A	0020037	molecular_function	heme binding
A	0031175	biological_process	neuron projection development
A	0043066	biological_process	negative regulation of apoptotic process
A	0043085	biological_process	positive regulation of catalytic activity
A	0043204	cellular_component	perikaryon
A	0046872	molecular_function	metal ion binding
A	0070301	biological_process	cellular response to hydrogen peroxide
A	0071456	biological_process	cellular response to hypoxia
A	0098809	molecular_function	nitrite reductase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	binding site for residue HEM A 201

Chain	Residue
A	LEU41
A	VAL101
A	SER105
A	PHE106
A	VAL109
A	TYR137
A	VAL140
A	CMO202
A	ACT208
A	HOH345
A	HOH350
A	PHE42
A	TYR44
A	HIS64
A	LYS67
A	LYS67
A	VAL71
A	LEU92
A	HIS96

---

site_id	AC2
Number of Residues	4
Details	binding site for residue CMO A 202

Chain	Residue
A	PHE28
A	HIS64
A	VAL68
A	HEM201

---

site_id	AC3
Number of Residues	4
Details	binding site for residue FMT A 203

Chain	Residue
A	ARG3
A	GLU5
A	ILE9
A	ALA132

---

site_id	AC4
Number of Residues	4
Details	binding site for residue FMT A 204

Chain	Residue
A	SER107
A	GLU111
A	LEU114
A	SER134

---

site_id	AC5
Number of Residues	4
Details	binding site for residue FMT A 205

Chain	Residue
A	LEU38
A	VAL101
A	ARG102
A	SER105

---

site_id	AC6
Number of Residues	7
Details	binding site for residue ACT A 206

Chain	Residue
A	SER84
A	LEU85
A	GLU86
A	GLU87
A	TYR88
A	HOH329
A	HOH363

---

site_id	AC7
Number of Residues	6
Details	binding site for residue ACT A 207

Chain	Residue
A	GLU22
A	PRO59
A	LEU62
A	ASP63
A	ARG66
A	ACT209

---

site_id	AC8
Number of Residues	7
Details	binding site for residue ACT A 208

Chain	Residue
A	LYS67
A	LYS67
A	TYR88
A	HEM201
A	HOH313
A	HOH319
A	HOH319

---

site_id	AC9
Number of Residues	7
Details	binding site for residue ACT A 209

Chain	Residue
A	ASP63
A	ARG66
A	THR90
A	SER91
A	ARG94
A	ACT207
A	HOH347

---

site_id	AD1
Number of Residues	7
Details	binding site for residue GOL A 210

Chain	Residue
A	SER17
A	PRO20
A	ASP73
A	ASN78
A	SER84
A	HOH315
A	HOH326

---

site_id	AD2
Number of Residues	9
Details	binding site for residue GOL A 211

Chain	Residue
A	ARG18
A	SER19
A	PRO20
A	LEU21
A	GLU22
A	ARG66
A	HOH363
A	HOH370
A	HOH376

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Binding site: {"description":"distal binding residue; reversible","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15162488","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Q1F","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Binding site: {"description":"proximal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15162488","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15548613","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Q1F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1W92","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---