Structure of PDB 1m9r Chain A

Receptor sequence
>1m9rA (length=400) Species: 9606 (Homo sapiens) [Search protein sequence]
KFPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPEQLLSQARDF
INQYYSSIKRSGSQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQAWRN
APRCVGRIQWGKLQVFDARDCRSAQEMFTYICNHIKYATNRGNLRSAITV
FPQRCPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGWT
PGNGRFDVLPLLLQAPDEPPELFLLPPELVLEVPLEHPTLEWFAALGLRW
YALPAVSNMLLEIGGLEFPAAPFSGWYMSTEIGTRNLCDPHRYNILEDVA
VCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDHHAATASFMKH
LENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPDPW
3D structure
PDB1m9r Conformational Changes in Nitric Oxide Synthases Induced by Chlorzoxazone and Nitroindazoles: Crystallographic and Computational Analyses of Inhibitor Potency
ChainA
Resolution2.56 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 A C94 C99 C28 C33
BS02 HEM A W178 C184 M339 F353 S354 W356 E361 F473 Y475 W98 C104 M259 F273 S274 W276 E281 F393 Y395
BS03 INE A P334 F353 S354 G355 W356 Y357 M358 E361 P254 F273 S274 G275 W276 Y277 M278 E281
BS04 INE A W445 F460 H461 Q462 E463 W365 F380 H381 Q382 E383
BS05 INE A R365 W447 R285 W367
Gene Ontology
Molecular Function
GO:0004517 nitric-oxide synthase activity
GO:0020037 heme binding
Biological Process
GO:0006809 nitric oxide biosynthetic process

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Molecular Function

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Biological Process
External links
PDB RCSB:1m9r, PDBe:1m9r, PDBj:1m9r
PDBsum1m9r
PubMed12437348
UniProtP29474|NOS3_HUMAN Nitric oxide synthase 3 (Gene Name=NOS3)

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