Structure of PDB 1p6m Chain B

Receptor sequence
>1p6mB (length=402) Species: 9913 (Bos taurus) [Search protein sequence]
KFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPRAEQLLSQAR
DFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYHLRESELVFGAKQAW
RNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNHIKYATNRGNLRSAI
TVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHG
WTPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVPLEHPTLEWFAALGL
RWYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGTRNLCDPHRYNILED
VAVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAKVTIVDHHAATVSFM
KHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYILSPAFRYQPD
PW
3D structure
PDB1p6m Structural basis for dipeptide amide isoform-selective inhibition of neuronal nitric oxide synthase.
ChainB
Resolution2.27 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C186 R189 W358 E363
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 H4B B W447 F462 H463 Q464 W367 F382 H383 Q384
BS02 ZN B C96 C101 C28 C33
BS03 HEM B W180 R185 C186 F355 W358 E363 W449 F475 Y477 W100 R105 C106 F275 W278 E283 W369 F395 Y397
BS04 H4B B S104 R367 A448 W449 S36 R287 A368 W369
BS05 DP3 B V338 W358 E363 V258 W278 E283 MOAD: Ki=80uM
Gene Ontology
Molecular Function
GO:0004517 nitric-oxide synthase activity
GO:0020037 heme binding
Biological Process
GO:0006809 nitric oxide biosynthetic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1p6m, PDBe:1p6m, PDBj:1p6m
PDBsum1p6m
PubMed14718923
UniProtP29473|NOS3_BOVIN Nitric oxide synthase 3 (Gene Name=NOS3)

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