Structure of PDB 3hsp Chain A

Receptor sequence

>3hspA (length=412) Species: 10116 (Rattus norvegicus)

RFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPSVRTKDQLFP
LAKEFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQLKDTELIYGAK
HAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLR
SAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICI
QQGWKAPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFDWFKD
LGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNI
LEEVAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATE
SFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEY
QPDPWNTHVWKG

3D structure

• PDB: 3hsp Single crystal structural and absorption spectral characterizations of nitric oxide synthase complexed with N(omega)-hydroxy-L-arginine and diatomic ligands.
• Chain: A
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C415 R418 W587 E592
• Catalytic site (residue number reindexed from 1): C109 R112 W281 E286
• 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	HEM	A	W409 R414 C415 V416 G417 F584 G586 W587 E592 W678 F704 Y706	W103 R108 C109 V110 G111 F278 G280 W281 E286 W372 F398 Y400
BS02	H4B	A	S334 R596 V677 W678	S36 R290 V371 W372
BS03	HAR	A	Q478 P565 V567 G586 W587 Y588 E592 D597	Q172 P259 V261 G280 W281 Y282 E286 D291
BS04	ZN	A	C326 C331	C28 C33
BS05	H4B	A	F691 E694	F385 E388

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

• PDB: RCSB:3hsp, PDBe:3hsp, PDBj:3hsp
• PDBsum: 3hsp
• PubMed: 19791770
• UniProt: P29476|NOS1_RAT Nitric oxide synthase 1 (Gene Name=Nos1)