Structure of PDB 2g6n Chain B

Receptor sequence

>2g6nB (length=411) Species: 10116 (Rattus norvegicus)

RFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPVRTKDQLFPL
AKEFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQLKDTELIYGAKH
AWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRS
AITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQ
QGWKAPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFDWFKDL
GLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNIL
EEVAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATES
FIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQ
PDPWNTHVWKG

3D structure

• PDB: 2g6n Structural studies of constitutive nitric oxide synthases with diatomic ligands bound.
• Chain: B
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C415 R418 W587 E592
• Catalytic site (residue number reindexed from 1): C108 R111 W280 E285
• Enzyme Commision number: 1.14.13.39: nitric-oxide synthase (NADPH).

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	ZN	B	C326 C331	C28 C33
BS02	HBI	B	F691 H692 Q693 E694	F384 H385 Q386 E387
BS03	HEM	B	W409 C415 V416 M570 F584 G586 W587 E592 W678 F704 Y706	W102 C108 V109 M263 F277 G279 W280 E285 W371 F397 Y399
BS04	HBI	B	S334 M336 R596 V677 W678	S36 M38 R289 V370 W371
BS05	ARG	B	Q478 P565 V567 Y588 E592 D597	Q171 P258 V260 Y281 E285 D290

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity
• GO:0020037 heme binding

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

• PDB: RCSB:2g6n, PDBe:2g6n, PDBj:2g6n
• PDBsum: 2g6n
• PubMed: 16804678
• UniProt: P29476|NOS1_RAT Nitric oxide synthase 1 (Gene Name=Nos1)