Structure of PDB 2g6l Chain B

Receptor sequence
>2g6lB (length=411) Species: 10116 (Rattus norvegicus) [Search protein sequence]
RFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPVRTKDQLFPL
AKEFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQLKDTELIYGAKH
AWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRS
AITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQ
QGWKAPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFDWFKDL
GLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNIL
EEVAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATES
FIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQ
PDPWNTHVWKG
3D structure
PDB2g6l Structural studies of constitutive nitric oxide synthases with diatomic ligands bound.
ChainB
Resolution2.05 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C415 R418 W587 E592
Catalytic site (residue number reindexed from 1) C108 R111 W280 E285
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 ZN B C326 C331 C28 C33
BS02 HBI B F691 E694 F384 E387
BS03 HEM B W409 C415 V416 F584 G586 W587 E592 W678 F704 Y706 W102 C108 V109 F277 G279 W280 E285 W371 F397 Y399
BS04 HBI B S334 R596 V677 W678 S36 R289 V370 W371
BS05 ARG B Q478 P565 W587 Y588 E592 D597 Q171 P258 W280 Y281 E285 D290
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:2g6l, PDBe:2g6l, PDBj:2g6l
PDBsum2g6l
PubMed16804678
UniProtP29476|NOS1_RAT Nitric oxide synthase 1 (Gene Name=Nos1)

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