Structure of PDB 1vaf Chain A

Receptor sequence

>1vafA (length=419) Species: 10090 (Mus musculus)

QYVRIKNWGSGEILHDTLHHKATSDFTCKSKSCLGSIMNPKSLTRGPRDK
PTPLEELLPHAIEFINQYYGSFKEAKIEEHLARLEAVTKEIETTGTYQLT
LDELIFATKMAWRNAPRCIGRIQWSNLQVFDARNCSTAQEMFQHICRHIL
YATNNGNIRSAITVFPQRSDGKHDFRLWNSQLIRYAGYQMPDGTIRGDAA
TLEFTQLCIDLGWKPRYGRFDVLPLVLQADGQDPEVFEIPPDLVLEVTME
HPKYEWFQELGLKWYALPAVANMLLEVGGLEFPACPFNGWYMGTEIGVRD
FCDTQRYNILEEVGRRMGLETHTLASLWKDRAVTEINVAVLHSFQKQNVT
IMDHHTASESFMKHMQNEYRARGGCPADWIWLVPPVSGSITPVFHQEMLN
YVLSPFYYYQIEPWKTHIW

3D structure

• PDB: 1vaf Structures of nitric oxide synthase isoforms complexed with the inhibitor AR-R17477 suggest a rational basis for specificity and inhibitor design
• Chain: A
• Resolution: 2.9 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	A	W188 C194 F363 N364 W366 E371 W457 Y485	W112 C118 F287 N288 W290 E295 W381 Y409
BS02	H4B	A	S112 M114 R375 I456 W457	S36 M38 R299 I380 W381
BS03	ARR	A	P344 V346 N348 F363 N364 G365 E371 Y485	P268 V270 N272 F287 N288 G289 E295 Y409	BindingDB: IC50=5000nM

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:1vaf, PDBe:1vaf, PDBj:1vaf
• PDBsum: 1vaf
• PubMed: 15071192
• UniProt: P29477|NOS2_MOUSE Nitric oxide synthase, inducible (Gene Name=Nos2)