Structure of PDB 3dqr Chain A

Receptor sequence
>3dqrA (length=407) Species: 10116 (Rattus norvegicus) [Search protein sequence]
RFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIVLPTKDQLFPLAK
EFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQLKDTELIYGAKHAW
RNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAI
TIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQG
WKAPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFDWFKDLGL
KWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRNYCDNSRYNILEE
VAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFI
KHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPD
PWNTHVW
3D structure
PDB3dqr Crystal structures of constitutive nitric oxide synthases in complex with de novo designed inhibitors.
ChainA
Resolution2.4 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) C106 R109 W278 E283
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 HEM A W409 C415 M570 F584 S585 W587 E592 W678 Y706 W100 C106 M261 F275 S276 W278 E283 W369 Y397
BS02 H4B A S334 R596 V677 W678 S36 R287 V368 W369
BS03 JI2 A V567 W587 E592 V258 W278 E283 MOAD: Ki=0.388uM
BindingDB: Ki=388nM,IC50=6300nM
BS04 ZN A C326 C331 C28 C33
BS05 H4B A F691 H692 E694 F382 H383 E385
Gene Ontology
Molecular Function
GO:0004517 nitric-oxide synthase activity
Biological Process
GO:0006809 nitric oxide biosynthetic process

View graph for
Molecular Function
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Biological Process
External links
PDB RCSB:3dqr, PDBe:3dqr, PDBj:3dqr
PDBsum3dqr
PubMed19296678
UniProtP29476|NOS1_RAT Nitric oxide synthase 1 (Gene Name=Nos1)

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