Structure of PDB 4uqs Chain A

Receptor sequence
>4uqsA (length=362) Species: 1423 (Bacillus subtilis) [Search protein sequence]
EEKEILWNEAKAFIAACYQELGKAAEVKDRLADIKSEIDLTGSYVHTKEE
LEHGAKMAWRNSNRCIGRLFWNSLNVIDRRDVRTKEEVRDALFHHIETAT
NNGKIRPTITIFPPEEKGEKQVEIWNHQLIRYAGYESDGERIGDPASCSL
TAACEELGWRGERTDFDLLPLIFRMKGDEQPVWYELPRSLVIEVPITHPD
IEAFSDLELKWYGVPIISDMKLEVGGIHYNAAPFNGWYMGTEIGARNLAD
EKRYDKLKKVASVIGIAADYNTDLWKDQALVELNKAVLHSYKKQGVSIVD
HHTAASQFKRFEEQAEEAGRKLTGDWTWLIPPISPAATHIFHRSYDNSIV
KPNYFYQDKPYE
3D structure
PDB4uqs Identification of Redox Partners and Development of a Novel Chimeric Bacterial Nitric Oxide Synthase for Structure Activity Analyses.
ChainA
Resolution2.15 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 S63 R65 C66 F235 N236 G237 W238 E243 W329 Y357 W59 S62 R64 C65 F234 N235 G236 W237 E242 W328 Y356
BS02 INE A P216 F235 N236 G237 W238 Y239 E243 P215 F234 N235 G236 W237 Y238 E242
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:4uqs, PDBe:4uqs, PDBj:4uqs
PDBsum4uqs
PubMed25194416
UniProtO34453|NOSO_BACSU Nitric oxide synthase oxygenase (Gene Name=nos)

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