Structure of PDB 3b3p Chain B

Receptor sequence
>3b3pB (length=411) Species: 10116 (Rattus norvegicus) [Search protein sequence]
RFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPVRTKDQLFPL
AKEFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQLKDTELIYGAKH
AWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRS
AITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQ
QGWKAPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFDWFKDL
GLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNIL
EEVAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATES
FIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQ
PDPWNTHVWKG
3D structure
PDB3b3p Crystal structures of constitutive nitric oxide synthases in complex with de novo designed inhibitors.
ChainB
Resolution2.45 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) 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 W676 F691 H692 E694 W369 F384 H385 E387
BS02 HEM B W409 C415 F584 W587 E592 W678 Y706 W102 C108 F277 W280 E285 W371 Y399
BS03 H4B B M336 R596 V677 W678 M38 R289 V370 W371
BS04 JI7 B L337 Q478 P565 F584 W587 E592 L39 Q171 P258 F277 W280 E285 MOAD: Ki=0.25uM
BindingDB: IC50=3300nM,Ki=250nM
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:3b3p, PDBe:3b3p, PDBj:3b3p
PDBsum3b3p
PubMed19296678
UniProtP29476|NOS1_RAT Nitric oxide synthase 1 (Gene Name=Nos1)

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