Structure of PDB 1dww Chain B

Receptor sequence

>1dwwB (length=420) Species: 10090 (Mus musculus)

QYVRIKNWGSGEILHDTLHHKATSDFTCKSKSCLGSIMNPKSLTRGPRDK
PTPLEELLPHAIEFINQYYGSFKEAKIEEHLARLEAVTKEIETTGTYQLT
LDELIFATKMAWRNAPRCIGRIQWSNLQVFDARNCSTAQEMFQHICRHIL
YATNNGNIRSAITVFPQRSDGKHDFRLWNSQLIRYAGYQMPDGTIRGDAA
TLEFTQLCIDLGWKPRYGRFDVLPLVLQADGQDPEVFEIPPDLVLEVTME
HPKYEWFQELGLKWYALPAVANMLLEVGGLEFPACPFNGWYMGTEIGVRD
FCDTQRYNILEEVGRRMGLETHTLASLWKDRAVTEINVAVLHSFQKQNVT
IMDHHTASESFMKHMQNEYRARGGCPADWIWLVPPVSGSITPVFHQEMLN
YVLSPFYYYQIEPWKTHIWQ

3D structure

• PDB: 1dww Structures of the N(Omega)-Hydroxy-L-Arginine Complex of Inducible Nitric Oxide Synthase Oxygenase Dimer with Active Andinactive Pterins
• Chain: B
• Resolution: 2.35 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C194 R197 W366 E371
• Catalytic site (residue number reindexed from 1): C118 R121 W290 E295
• 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 C194 F363 N364 G365 W366 E371 W457 Y483 Y485	W112 C118 F287 N288 G289 W290 E295 W381 Y407 Y409
BS02	H2B	B	R375 I456 W457	R299 I380 W381
BS03	ZN	B	C104 C109	C28 C33
BS04	HAR	B	Q257 P344 G365 W366 Y367 E371 D376	Q181 P268 G289 W290 Y291 E295 D300

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity
• GO:0020037 heme binding

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

• PDB: RCSB:1dww, PDBe:1dww, PDBj:1dww
• PDBsum: 1dww
• PubMed: 10769116
• UniProt: P29477|NOS2_MOUSE Nitric oxide synthase, inducible (Gene Name=Nos2)