Structure of PDB 1vag Chain A

Receptor sequence

>1vagA (length=420) Species: 10116 (Rattus norvegicus)

GPRFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPSQHTRKPE
DVRTKDQLFPLAKEFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQL
KDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHV
KYATNKGNLRSAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDP
ANVQFTEICIQQGWKAPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPI
RHPKFDWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVR
DYCDNSRYNILEEVAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKV
TIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEML
NYRLTPSFEYQPDPWNTHVW

3D structure

• PDB: 1vag Structures of nitric oxide synthase isoforms complexed with the inhibitor AR-R17477 suggest a rational basis for specificity and inhibitor design
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C415 R418 W587 E592
• Catalytic site (residue number reindexed from 1): C119 R122 W291 E296
• 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	A	C326 C331	C30 C35
BS02	HEM	A	W409 C415 Q420 F584 W587 E592 W678 F704 Y706	W113 C119 Q124 F288 W291 E296 W382 F408 Y410
BS03	H4B	A	S334 R596 V677 W678	S38 R300 V381 W382
BS04	ARR	A	L337 P565 V567 F584 S585 G586 E592 Y706	L41 P269 V271 F288 S289 G290 E296 Y410	BindingDB: IC50=120nM

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:1vag, PDBe:1vag, PDBj:1vag
• PDBsum: 1vag
• PubMed: 15071192
• UniProt: P29476|NOS1_RAT Nitric oxide synthase 1 (Gene Name=Nos1)