Structure of PDB 4ugh Chain A

Receptor sequence
>4ughA (length=362) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence]
EEKEILWNEAKAFIAACYQELGKAAEVKDRLADIKSEIDLTGSYVHTKEE
LEHGAKMAWRNSNRCIGRLFWNSLNVIDRRDVRTKEEVRDALFHHIETAT
NNGKIRPTITIFPPEEKGEKQVEIWNHQLIRYAGYESDGERIGDPASCSL
TAACEELGWRGERTDFDLLPLIFRMKGDEQPVWYELPRSLVIEVPITHPD
IEAFSDLELKWYGVPIISDMKLEVGGIHYNAAPFNGWYMGTEIGARNLAD
EKRYDKLKKVASVIGIAADYNTDLWKDQALVELNKAVLHSYKKQGVSIVD
HHTAASQFKRFEEQAEEAGRKLTGDWTWLIPPISPAATHIFHRSYDNSIV
KPNYFYQDKPYE
3D structure
PDB4ugh Inhibitor Bound Crystal Structures of Bacterial Nitric Oxide Synthase.
ChainA
Resolution1.994 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C66 R69 W238 E243
Catalytic site (residue number reindexed from 1) C65 R68 W237 E242
Enzyme Commision number 1.14.14.47: nitric-oxide synthase (flavodoxin).
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 W60 R65 C66 F235 N236 G237 W238 E243 W329 Y355 Y357 W59 R64 C65 F234 N235 G236 W237 E242 W328 Y354 Y356
BS02 H4B A R247 T328 W329 R246 T327 W328
BS03 4V4 A H128 Q129 I218 F235 E243 H127 Q128 I217 F234 E242 BindingDB: Kd=5.046e+4nM
Gene Ontology
Molecular Function
GO:0004517 nitric-oxide synthase activity
GO:0016491 oxidoreductase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0006809 nitric oxide biosynthetic process
Cellular Component
GO:0005575 cellular_component

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4ugh, PDBe:4ugh, PDBj:4ugh
PDBsum4ugh
PubMed26062720
UniProtO34453|NOSO_BACSU Nitric oxide synthase oxygenase (Gene Name=nos)

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