Structure of PDB 4cx5 Chain B

Receptor sequence

>4cx5B (length=411) Species: 10116 (Rattus norvegicus)

RFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPVRTKDQLFPL
AKEFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQLKDTELIYGAKH
AWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRS
AITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQ
QGWKAPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFDWFKDL
GLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNIL
EEVAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATES
FIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQ
PDPWNTHVWKG

3D structure

• PDB: 4cx5 Mobility of a Conserved Tyrosine Residue Controls Isoform-Dependent Enzyme-Inhibitor Interactions in Nitric Oxide Synthases.
• Chain: B
• Resolution: 1.8 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	H4B	B	F691 E694	F384 E387
BS02	ZN	B	C326 C331	C28 C33
BS03	HEM	B	W409 C415 G417 M570 F584 W587 E592 F704	W102 C108 G110 M263 F277 W280 E285 F397
BS04	H4B	B	S334 R596 V677 W678	S36 R289 V370 W371
BS05	HW8	B	M336 Q478 P565 W587 E592 W678 Y706	M38 Q171 P258 W280 E285 W371 Y399	BindingDB: Kd=212nM

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

• PDB: RCSB:4cx5, PDBe:4cx5, PDBj:4cx5
• PDBsum: 4cx5
• PubMed: 25089924
• UniProt: P29476|NOS1_RAT Nitric oxide synthase 1 (Gene Name=Nos1)