1GVH

The X-ray structure of ferric Escherichia coli flavohemoglobin reveals an unespected geometry of the distal heme pocket

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005344	molecular_function	oxygen carrier activity
A	0005504	molecular_function	fatty acid binding
A	0005737	cellular_component	cytoplasm
A	0008941	molecular_function	nitric oxide dioxygenase [NAD(P)H] activity
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	0046210	biological_process	nitric oxide catabolic process
A	0051409	biological_process	response to nitrosative stress
A	0071500	biological_process	cellular response to nitrosative stress
A	0071949	molecular_function	FAD binding
A	0098869	biological_process	cellular oxidant detoxification

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA A 1399

Chain	Residue
A	LYS40
A	PHE43
A	GLN201
A	GLU202

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA A 1400

Chain	Residue
A	GLN271
A	HIS294
A	HIS302
A	ALA303
A	HOH2137

---

site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 1401

Chain	Residue
A	GLY51

---

site_id	AC4
Number of Residues	27
Details	BINDING SITE FOR RESIDUE FAD A 1397

Chain	Residue
A	ASN44
A	SER46
A	GLN48
A	ASN50
A	TYR188
A	ARG204
A	GLN205
A	TYR206
A	SER207
A	ALA220
A	VAL221
A	LYS222
A	GLU224
A	GLU225
A	GLY227
A	GLN228
A	VAL229
A	SER230
A	VAL269
A	THR272
A	GLU388
A	PHE390
A	HOH2095
A	HOH2103
A	HOH2187
A	HOH2188
A	HOH2189

---

site_id	AC5
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEM A 1398

Chain	Residue
A	LEU39
A	ASN44
A	GLN53
A	ALA56
A	LEU57
A	ALA60
A	ILE61
A	ILE81
A	LYS84
A	HIS85
A	PHE88
A	ILE90
A	GLN94
A	TYR95
A	VAL98
A	LEU127
A	PRO392
A	HIS393
A	HOH2190
A	HOH2191

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	135
Details	Domain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	105
Details	Domain: {"description":"FAD-binding FR-type"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	249
Details	Region: {"description":"Reductase"}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"11092893","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	17
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11964402","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GVH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Binding site: {"description":"proximal binding residue","evidences":[{"source":"PubMed","id":"11964402","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GVH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P39662","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	5
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Site: {"description":"Involved in heme-bound ligand stabilization and O-O bond activation"}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	Site: {"description":"Influences the redox potential of the prosthetic heme and FAD groups"}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1ndh

Chain	Residue	Details
A	TYR206

---