Brand  (β version)

PDB ID: 1P6L

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Ligands
Code Name Style Show Link
ACT Acetate ion PoSSuM
CAC Cacodylate ion PoSSuM
DP1 L-N(omega)-nitroarginine-2,4-L-diaminobutyric amide PoSSuM
GOL Glycerol PoSSuM
H4B 5,6,7,8-tetrahydrobiopterin PoSSuM
HEM Protoporphyrin ix containing Fe PoSSuM
ZN Zinc ion PoSSuM
Non-standard Residues
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Structure summary

Code : 1P6L   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : Bovine endothelial NOS heme domain with L-N(omega)-nitroarginine-2,4-L-diaminobutyric amide bound
Release Data : 2004-01-13
Compound :
mol_id molecule chains synonym
1 Nitric-oxide synthase, endothelial A,B EC-NOS, NOS, type III, NOSIII, Endothelial NOS, eNOS, Constitutive NOS, cNOS
ec: 1.14.13.39
fragment: NOS HEME DOMAIN
Source :
mol_id organism_scientific organism_common expression_system
1 Bos taurus  (taxid:9913) Cattle Pichia pastoris  (taxid:4922)
gene: endothelial nitric oxide synthase
expression_system_strain: KM71H
expression_system_vector_type: plasmid
expression_system_plasmid: pPICZ
Authors : Flinspach, M.L., Li, H., Jamal, J., Yang, W., Huang, H., Hah, J.-M., Gomez-Vidal, J.A., Litzinger, E.A., Silverman, R.B., Poulos, T.L.
Keywords : nitric oxide synthase, oxidoreductase, heme-enzyme
Exp. method : X-RAY DIFFRACTION ( 2.35 Å )
Citation :

Structural basis for dipeptide amide isoform-selective inhibition of neuronal nitric oxide synthase.

Flinspach, M.L.,Li, H.,Jamal, J.  et al.
(2004)  Nat.Struct.Mol.Biol.  11 : 54 - 59

PubMed: 14718923
DOI: 10.1038/nsmb704

CRYSTAL STRUCTURE OF CONSTITUTIVE ENDOTHELIAL NITRIC OXIDE SYNTHASE: A PARADIGM FOR PTERIN FUNCTION INVOLVING A NOVEL METAL CENTER

Raman, C.S.,Li, H.,Martasek, P.  et al.
(1998)  Cell(Cambridge,Mass.)  95 : 939 - 950

DOI: 10.1016/S0092-8674(00)81718-3

The novel binding mode of N-alkyl-N'-hydroxyguanidine to neuronal nitric oxide synthase provides mechanistic insights into NO biosynthesis

Li, H.,Shimizu, H.,Flinspach, M.  et al.
(2002)  Biochemistry  41 : 13868 - 13875

DOI: 10.1021/bi020417c

Reaction

Chain : A, B
UniProt : P29473 (NOS3_BOVIN)
Reaction: EC: Evidence:
Physiological Direction:
2 L-arginine + 3 NADPH + 4 O2 + H(+) = 2 L-citrulline + 2 nitric oxide + 3 NADP(+) + 4 H2O 1.14.13.39 UniProtKB:P29474
left-to-right
Cofactor: Evidence: Note:
heme b ECO:0000269 | PubMed:11051558
ECO:0000269 | PubMed:9875848
-
FAD ECO:0000250 | UniProtKB:P29476
Binds 1 FAD.
FMN ECO:0000250 | UniProtKB:P35228
Binds 1 FMN.
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin ECO:0000269 | PubMed:11051558
ECO:0000269 | PubMed:11331003
ECO:0000269 | PubMed:9875848
Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme.