Structure of PDB 4ugd Chain A

Receptor sequence
>4ugdA (length=362) Species: 1423 (Bacillus subtilis) [Search protein sequence]
EEKEILWNEAKAFIAACYQELGKAAEVKDRLADIKSEIDLTGSYVHTKEE
LEHGAKMAWRNSNRCIGRLFWNSLNVIDRRDVRTKEEVRDALFHHIETAT
NNGKIRPTITIFPPEEKGEKQVEIWNHQLIRYAGYESDGERIGDPASCSL
TAACEELGWRGERTDFDLLPLIFRMKGDEQPVWYELPRSLVIEVPITHPD
IEAFSDLELKWYGVPIISDMKLEVGGIHYNAAPFNGWYMGTEIGARNLAD
EKRYDKLKKVASVIGIAADYNTDLWKDQALVELNKAVLHSYKKQGVSIVD
HHTAASQFKRFEEQAEEAGRKLTGDWTWLIPPISPAATHIFHRSYDNSIV
KPNYFYQDKPYE
3D structure
PDB4ugd Inhibitor Bound Crystal Structures of Bacterial Nitric Oxide Synthase.
ChainA
Resolution2.03 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 Y355 Y357 W59 R64 C65 F234 N235 G236 W237 E242 Y354 Y356
BS02 H4B A T328 W329 T327 W328
BS03 Q14 A I218 F235 W238 E243 Y357 I217 F234 W237 E242 Y356 BindingDB: Kd=3.79e+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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4ugd, PDBe:4ugd, PDBj:4ugd
PDBsum4ugd
PubMed26062720
UniProtO34453|NOSO_BACSU Nitric oxide synthase oxygenase (Gene Name=nos)

[Back to BioLiP]