Brand  (β version)

PDB ID: 1D1Y

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Ligands
Code Name Style Show Link
3BT 2-{2-[3-(2-carbamimidoylsulfanyl-ethyl)-phenyl]-ethyl}-isothiourea PoSSuM
ACT Acetate ion PoSSuM
CAD Cacodylic acid PoSSuM
EDO 1,2-ethanediol PoSSuM
GOL Glycerol PoSSuM
HEM Protoporphyrin ix containing Fe PoSSuM
ZN Zinc ion PoSSuM
Non-standard Residues
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Structure summary

Code : 1D1Y   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH 1,3-PBITU (H4B FREE)
Release Data : 2001-07-25
Compound :
mol_id molecule chains
1 BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN A,B
ec: 1.14.13.39
Source :
mol_id organism_scientific organism_common expression_system
1 Bos taurus  (taxid:9913) Cattle Escherichia coli  (taxid:562)
cell: ENDOTHELIAL CELLS
Authors : Raman, C.S., Li, H., Martasek, P., Southan, G.J., Masters, B.S.S., Poulos, T.L.
Keywords : ALPHA-BETA FOLD, oxidoreductase
Exp. method : X-RAY DIFFRACTION ( 2.20 Å )
Citation :

Implications for isoform-selective inhibitor design derived from the binding mode of bulky isothioureas to the heme domain of endothelial nitric-oxide synthase.

Raman, C.S.,Li, H.,Martasek, P.  et al.
(2001)  J.Biol.Chem.  276 : 26486 - 26491

PubMed: 11331290
DOI: 10.1074/jbc.M102255200

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

Structure of Nitric Oxide Synthase Oxygenase Dimer with Pterin and Substrate

Crane, B.R.,Arvai, A.S.,Ghosh, D.K.  et al.
(1998)  Science  279 : 2121 - 2126

DOI: 10.1126/science.279.5359.2121

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.