Structure of PDB 3nlj Chain A

Receptor sequence
>3nljA (length=407) Species: 10116 (Rattus norvegicus) [Search protein sequence]
RFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIVLPTKDQLFPLAK
EFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQLKDTELIYGAKHAW
RNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAI
TIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQG
WKAPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFDWFKDLGL
KWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRNYCDNSRYNILEE
VAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFI
KHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEAQPD
PWNTHVW
3D structure
PDB3nlj Exploration of the Active Site of Neuronal Nitric Oxide Synthase by the Design and Synthesis of Pyrrolidinomethyl 2-Aminopyridine Derivatives.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 HEM A W409 C415 M570 F584 S585 G586 W587 W678 F704 W100 C106 M261 F275 S276 G277 W278 W369 F395
BS02 H4B A S334 R596 V677 W678 S36 R287 V368 W369
BS03 JRR A Q478 P565 V567 S585 E592 Q169 P256 V258 S276 E283 BindingDB: Ki=7.0nM,IC50=100nM
BS04 H4B A F691 E694 F382 E385
Gene Ontology
Molecular Function
GO:0004517 nitric-oxide synthase activity
Biological Process
GO:0006809 nitric oxide biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3nlj, PDBe:3nlj, PDBj:3nlj
PDBsum3nlj
PubMed20958055
UniProtP29476|NOS1_RAT Nitric oxide synthase 1 (Gene Name=Nos1)

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