Structure of PDB 1k2u Chain B

Receptor sequence

>1k2uB (length=410) Species: 10116 (Rattus norvegicus)

RFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPVRTKDQLFPL
AKEFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQLKDTELIYGAKH
AWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRS
AITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQ
QGWKAPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFDWFKDL
GLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNIL
EEVAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATES
FIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQ
PDPWNTHVWK

3D structure

• PDB: 1k2u Crystal structure of constitutive endothelial nitric oxide synthase: a paradigm for pterin function involving a novel metal center
• Chain: B
• Resolution: 2.2 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	H4B	B	F691 H692 Q693 E694	F384 H385 Q386 E387
BS03	HEM	B	W409 R414 C415 M570 F584 W587 E592 W678 Y706	W102 R107 C108 M263 F277 W280 E285 W371 Y399
BS04	H4B	B	S334 R596 V677 W678	S36 R289 V370 W371
BS05	TFM	B	P565 V567 F584 W587 E592	P258 V260 F277 W280 E285

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:1k2u, PDBe:1k2u, PDBj:1k2u
• PDBsum: 1k2u
• UniProt: P29476|NOS1_RAT Nitric oxide synthase 1 (Gene Name=Nos1)