Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
ACT Acetate ion
H4B 5,6,7,8-tetrahydrobiopterin
HEM Protoporphyrin ix containing Fe
HW9 4-methyl-6-{[(3r,4r)-4-{[5-(4-methylpyridin-2-yl)pentyl]oxy}pyrrolidin-3-yl]methyl}pyridin-2-amine
ZN Zinc ion
Non-standard Residues
Code Name Show
CAS S-(dimethylarsenic)cysteine
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 4CWW   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : Structure of bovine endothelial nitric oxide synthase heme domain in complex with 4-METHYL-6-(((3R,4R)-4-((5-(4-METHYLPYRIDIN-2-YL)PENTYL) OXY)PYRROLIDIN-3-YL)METHYL)PYRIDIN-2-AMINE
Release Data : 2014-08-13
Compound :
mol_id molecule chains synonym
1 NITRIC OXIDE SYNTHASE, ENDOTHELIAL A,B CONSTITUTIVE NOS, CNOS, EC-NOS, ENDOTHELIAL NOS, ENOS, NOS TYPE III, NOSIII, ENDOTHELIAL NITRIC OXIDE SYNTHASE
ec: 1.14.13.39
fragment: HEME DOMAIN, RESIDUES 40-482
Source :
mol_id organism_scientific organism_common expression_system
1 BOS TAURUS  (taxid:9913) CATTLE ESCHERICHIA COLI  (taxid:469008)
expression_system_strain: BL21(DE3)
expression_system_vector_type: PLASMID
expression_system_vector: PCWORI
Authors : Li, H., Poulos, T.L.
Keywords : OXIDOREDUCTASE, NITRIC OXIDE SYNTHASE, INHIBITOR COMPLEX
Exp. method : X-RAY DIFFRACTION ( 2.16 Å )
Citation :

Mobility of a Conserved Tyrosine Residue Controls Isoform-Dependent Enzyme-Inhibitor Interactions in Nitric Oxide Synthases.

Li, H.,Jamal, J.,Delker, S.L.  et al.
(2014)  Biochemistry  53 : 5272

PubMed: 25089924
DOI: 10.1021/BI500561H

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.