Structure of PDB 3ozw Chain A

Receptor sequence

>3ozwA (length=403) Species: 381666 (Cupriavidus necator H16)

MLTQKTKDIVKATAPVLAEHGYDIIKCFYQRMFEAHPELKNVFNMAHQEQ
GQQQQALARAVYAYAENIEDPNSLMAVLKNIANKHASLGVKPEQYPIVGE
HLLAAIKEVLGNAATDDIISAWAQAYGNLADVLMGMESELYERSAEQPGG
WKGWRTFVIREKRPESDVITSFILEPADGGPVVNFEPGQYTSVAIDVPAL
GLQQIRQYSLSDMPNGRSYRISVKREGGGPQPPGYVSNLLHDHVNVGDQV
KLAAPYGSFHIDVDAKTPIVLISGGVGLTPMVSMLKVALQAPPRQVVFVH
GARNSAVHAMRDRLREAAKTYENLDLFVFYDQPLPEDVQGRDYDYPGLVD
VKQIEKSILLPDADYYICGPIPFMRMQHDALKNLGIHEARIHYEVFGPDL
FAE

3D structure

• PDB: 3ozw Structure of Ralstonia eutropha Flavohemoglobin in Complex with Three Antibiotic Azole Compounds.
• Chain: A
• Resolution: 2.3 Å

Enzymatic activity

• Enzyme Commision number: 1.14.12.17: nitric oxide dioxygenase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	HEM	A	V42 F43 I81 H85 L88 V90 Q94 Y95 V98 Y126 A130 L133	V42 F43 I81 H85 L88 V90 Q94 Y95 V98 Y126 A130 L133
BS02	FAD	A	A46 Q50 R206 Q207 Y208 S209 S222 V223 K224 E226 P232 G234 Y235 V236 S237 V276 T279 V395 F396	A46 Q50 R206 Q207 Y208 S209 S222 V223 K224 E226 P232 G234 Y235 V236 S237 V276 T279 V395 F396
BS03	KKK	A	Q53 A56 L102 P398	Q53 A56 L102 P398	MOAD: Kd=10.1uM

Gene Ontology

Molecular Function

• GO:0005344 oxygen carrier activity
• GO:0008941 nitric oxide dioxygenase NAD(P)H activity
• GO:0016491 oxidoreductase activity
• GO:0019825 oxygen binding
• GO:0020037 heme binding
• GO:0046872 metal ion binding
• GO:0071949 FAD binding

Biological Process

• GO:0009636 response to toxic substance
• GO:0015671 oxygen transport
• GO:0046210 nitric oxide catabolic process
• GO:0051409 response to nitrosative stress
• GO:0071500 cellular response to nitrosative stress

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:3ozw, PDBe:3ozw, PDBj:3ozw
• PDBsum: 3ozw
• PubMed: 21210640
• UniProt: P39662|HMP_CUPNH Flavohemoprotein (Gene Name=hmp)