Structure of PDB 1k2s Chain A Binding Site BS04

Receptor Information
>1k2s Chain A (length=407) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPTKDQLFPLAK
EFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQLKDTELIYGAKHAW
RNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAI
TIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQG
WKAPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFDWFKDLGL
KWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEE
VAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFI
KHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPD
PWNTHVW
Ligand information
Ligand IDARV
InChIInChI=1S/C9H18N4O2/c1-2-5-12-9(11)13-6-3-4-7(10)8(14)15/h2,7H,1,3-6,10H2,(H,14,15)(H3,11,12,13)/p+1/t7-/m0/s1
InChIKeyZPQWZDPOLXVMOU-ZETCQYMHSA-O
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C=CC[NH+]=C(N)NCCCC(C(=O)O)N
CACTVS 3.341N[CH](CCCNC(N)=[NH+]CC=C)C(O)=O
OpenEye OEToolkits 1.5.0C=CC\[NH+]=C(\N)/NCCC[C@@H](C(=O)O)N
CACTVS 3.341N[C@@H](CCCNC(N)=[NH+]CC=C)C(O)=O
ACDLabs 10.04O=C(O)C(N)CCCN\C(=[NH+]/C\C=C)N
FormulaC9 H19 N4 O2
Name5-N-ALLYL-ARGININE
ChEMBL
DrugBankDB03892
ZINC
PDB chain1k2s Chain A Residue 1780 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1k2s Crystal structure of constitutive endothelial nitric oxide synthase: a paradigm for pterin function involving a novel metal center
Resolution2.55 Å
Binding residue
(original residue number in PDB)		Q478 P565 V567 F584 Y588 E592 D597
Binding residue
(residue number reindexed from 1)		Q169 P256 V258 F275 Y279 E283 D288
Annotation score2
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).
Gene Ontology
Molecular Function
GO:0004517 nitric-oxide synthase activity
GO:0020037 heme binding
Biological Process
GO:0006809 nitric oxide biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1k2s, PDBe:1k2s, PDBj:1k2s
PDBsum1k2s
PubMed
UniProtP29476|NOS1_RAT Nitric oxide synthase 1 (Gene Name=Nos1)

[Back to BioLiP]