Structure of PDB 1tll Chain B

Receptor sequence
>1tllB (length=616) Species: 10116 (Rattus norvegicus) [Search protein sequence]
RVKATILYATETGKSQAYAKTLCEIFKHAFDAKAMSMEEYDIVHLEHEAL
VLVVTSTFGNGDPPENGEKFGCALMEMRSYKVRFNVRFSVFGLGSRAYPH
FCAFGHAVDTLLEELGGERILKMREGDELCGQEEAFRTWAKKVFKAACDV
FCVGDDVNIEKSNDRSWKRNKFRLTYVAEAPDLTQGLSNVHKKRVSAARL
LSRQNLQSPKSSRSTIFVRLHTNGNQELQYQPGDHLGVFPGNHEDLVNAL
IERLEDAPPANHVVKVEMLEERNTALGVISNWKDESRLPPCTIFQAFKYY
LDITTPPTPLQLQQFASLATNEKEKQRLLVLSKGLQEYEEWKWGKNPTMV
EVLEEFPSIQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIVSY
HTRDGEGPVHHGVCSSWLNRIQADDVVPCFVRGAPSFHLPRNPQVPCILV
GPGTGIAPFRSFWQQRQFDIQHKGMNPCPMVLVFGCRQSKIDHIYREETL
QAKNKGVFRELYTAYSREPDRPKKYVQDVLQEQLAESVYRALKEQGGHIY
VCGDVTMAADVLKAIQRIMTQQGKLSEEDAGVFISRLRDDNRYHEDIFGV
TLRTYEVTNRLRSESI
3D structure
PDB1tll Structural basis for isozyme-specific regulation of electron transfer in nitric-oxide synthase
ChainB
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y3175 S3176 C3349 D3393 F3395
Catalytic site (residue number reindexed from 1) Y378 S379 C552 D596 F598
Enzyme Commision number 1.14.13.39: nitric-oxide synthase (NADPH).
Interaction with ligand
Gene Ontology
Molecular Function
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity

View graph for
Molecular Function
External links
PDB RCSB:1tll, PDBe:1tll, PDBj:1tll
PDBsum1tll
PubMed15208315
UniProtP29476|NOS1_RAT Nitric oxide synthase 1 (Gene Name=Nos1)

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