Structure of PDB 1jwk Chain B

Receptor sequence
>1jwkB (length=412) Species: 10090 (Mus musculus) [Search protein sequence]
QYVRIKNWGSGEILHDTLHHKATCLGSIMNPKSLTRGPRDKPTPLEELLP
HAIEFINQYYGSFKEAKIEEHLARLEAVTKEIETTGTYQLTLDELIFATK
MAWRNAPRCIGRIQWSNLQVFDARNCSTAQEMFQHICRHILYATNNGNIR
SAITVFPQRSDGKHDFRLWNSQLIRYAGYQMPDGTIRGDAATLEFTQLCI
DLGWKPRYGRFDVLPLVLQADGQDPEVFEIPPDLVLEVTMEHPKYEWFQE
LGLKWYALPAVANMLLEVGGLEFPACPFNGWYMGTEIGVRDFCDTQRYNI
LEEVGRRMGLETHTLASLWKDRAVTEINVAVLHSFQKQNVTIMDHHTASE
SFMKHMQNEYRARGGCPADWIALVPPVSGSITPVFHQEMLNYVLSPFYYY
QIEPWKTHIWQN
3D structure
PDB1jwk Structures of tetrahydrobiopterin binding-site mutants of inducible nitric oxide synthase oxygenase dimer and implicated roles of Trp457.
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) C194 R197 W366 E371
Catalytic site (residue number reindexed from 1) C109 R112 W281 E286
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 B W188 R193 C194 S236 F363 N364 G365 W366 E371 Y485 W103 R108 C109 S151 F278 N279 G280 W281 E286 Y400
BS02 HBI B S112 M114 R193 R375 I456 A457 S27 M29 R108 R290 I371 A372
Gene Ontology
Molecular Function
GO:0004517 nitric-oxide synthase activity
Biological Process
GO:0006809 nitric oxide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1jwk, PDBe:1jwk, PDBj:1jwk
PDBsum1jwk
PubMed11669619
UniProtP29477|NOS2_MOUSE Nitric oxide synthase, inducible (Gene Name=Nos2)

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