Structure of PDB 1r35 Chain A

Receptor sequence
>1r35A (length=413) Species: 10090 (Mus musculus) [Search protein sequence]
QYVRIKNWGSGEILHDTLHHKATSSCLGSIMNPKSLTRGPRDKPTPLEEL
LPHAIEFINQYYGSFKEAKIEEHLARLEAVTKEIETTGTYQLTLDELIFA
TKMAWRNAPRCIGRIQWSNLQVFDARNCSTAQEMFQHICRHILYATNNGN
IRSAITVFPQRSDGKHDFRLWNSQLIRYAGYQMPDGTIRGDAATLEFTQL
CIDLGWKPRYGRFDVLPLVLQADGQDPEVFEIPPDLVLEVTMEHPKYEWF
QELGLKWYALPAVANMLLEVGGLEFPACPFNGWYMGTEIGVRDFCDTQRY
NILEEVGRRMGLETHTLASLWKDRAVTEINVAVLHSFQKQNVTIMDHHTA
SESFMKHMQNEYRARGGCPADWIWLVPPVSGSITPVFHQEMLNYVLSPFY
YYQIEPWKTHIWQ
3D structure
PDB1r35 4-Fluorinated L-lysine analogs as selective i-NOS inhibitors: methodology for introducing fluorine into the lysine side chain.
ChainA
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) C111 R114 W283 E288
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 W188 C194 I195 M349 F363 G365 W366 E371 W457 Y485 W105 C111 I112 M266 F280 G282 W283 E288 W374 Y402
BS02 H4B A S112 M114 R375 I456 W457 S29 M31 R292 I373 W374
BS03 I58 A Q257 P344 V346 W366 Y367 E371 D376 Q174 P261 V263 W283 Y284 E288 D293 MOAD: ic50=6.09uM
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:1r35, PDBe:1r35, PDBj:1r35
PDBsum1r35
PubMed14599013
UniProtP29477|NOS2_MOUSE Nitric oxide synthase, inducible (Gene Name=Nos2)

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