Structure of PDB 1k2s Chain A

Receptor sequence

>1k2sA (length=407) Species: 10116 (Rattus norvegicus)

RFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPTKDQLFPLAK
EFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQLKDTELIYGAKHAW
RNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAI
TIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQG
WKAPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFDWFKDLGL
KWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEE
VAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFI
KHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPD
PWNTHVW

3D structure

• PDB: 1k2s Crystal structure of constitutive endothelial nitric oxide synthase: a paradigm for pterin function involving a novel metal center
• Chain: A
• Resolution: 2.55 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C415 R418 W587 E592
• Catalytic site (residue number reindexed from 1): C106 R109 W278 E283
• 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	C28 C33
BS02	HEM	A	W409 C415 V416 M570 F584 W587 E592 W678 F704 Y706	W100 C106 V107 M261 F275 W278 E283 W369 F395 Y397
BS03	H4B	A	S334 R596 V677 W678	S36 R287 V368 W369
BS04	ARV	A	Q478 P565 V567 F584 Y588 E592 D597	Q169 P256 V258 F275 Y279 E283 D288
BS05	H4B	A	F691 H692	F382 H383

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:1k2s, PDBe:1k2s, PDBj:1k2s
• PDBsum: 1k2s
• UniProt: P29476|NOS1_RAT Nitric oxide synthase 1 (Gene Name=Nos1)