Structure of PDB 1m9r Chain B

Receptor sequence

>1m9rB (length=400) Species: 9606 (Homo sapiens)

KFPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPEQLLSQARDF
INQYYSSIKRSGSQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQAWRN
APRCVGRIQWGKLQVFDARDCRSAQEMFTYICNHIKYATNRGNLRSAITV
FPQRCPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGWT
PGNGRFDVLPLLLQAPDEPPELFLLPPELVLEVPLEHPTLEWFAALGLRW
YALPAVSNMLLEIGGLEFPAAPFSGWYMSTEIGTRNLCDPHRYNILEDVA
VCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDHHAATASFMKH
LENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPDPW

3D structure

• PDB: 1m9r Conformational Changes in Nitric Oxide Synthases Induced by Chlorzoxazone and Nitroindazoles: Crystallographic and Computational Analyses of Inhibitor Potency
• Chain: B
• Resolution: 2.56 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C184 R187 W356 E361
• Catalytic site (residue number reindexed from 1): C104 R107 W276 E281
• 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	ZN	B	C94 C99	C28 C33
BS02	INE	B	S102 R365 A446 W447	S36 R285 A366 W367
BS03	HEM	B	W178 C184 M339 F353 W356 E361 F473 Y475	W98 C104 M259 F273 W276 E281 F393 Y395
BS04	INE	B	P334 F353 S354 W356 Y357 E361	P254 F273 S274 W276 Y277 E281
BS05	INE	B	W74 F460 H461 E463	W8 F380 H381 E383

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:1m9r, PDBe:1m9r, PDBj:1m9r
• PDBsum: 1m9r
• PubMed: 12437348
• UniProt: P29474|NOS3_HUMAN Nitric oxide synthase 3 (Gene Name=NOS3)