Structure of PDB 2amo Chain A

Receptor sequence
>2amoA (length=362) Species: 1423 (Bacillus subtilis) [Search protein sequence]
SHAAILWNEAKAFIAECYAELGKAEEVADRLDSIKSEIDLTGSYVHTKEE
LEHGAKMAWRNSNRCIGRLFWNSLNVIDRRDVRTKEDVRDALFHHIETAT
NNGKIRPSITIFPPEEKGEKQVEIWNHQLIRYAGYEAAGEAIGDPASCSL
TAACEQLGWRGERTDFDLLPLIFRMKGDEQPVWYELPRSLVIEVPITHPD
IEAFSDLELKWYGVPIISDMKLEVGGIHYNAAPFNGWYMGTEIGARNLAD
EKRYDKLKKVASVIGISTNYNTDLWKDQALVELNKAVLYSYKKQGVSIVD
HHTAASQFKRFEEQEEEAGRKLTGDWTWLIPPISPAATHIFHRSYDNSIV
KPNYFYQDKPYE
3D structure
PDB2amo Structure of a loose dimer: an intermediate in nitric oxide synthase assembly.
ChainA
Resolution2.6 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) C62 R65 W234 E239
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 W56 C62 F231 N232 G233 W234 E239 W325 Y351 Y353 W59 C65 F234 N235 G236 W237 E242 W328 Y354 Y356
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:2amo, PDBe:2amo, PDBj:2amo
PDBsum2amo
PubMed16126221
UniProtO34453|NOSO_BACSU Nitric oxide synthase oxygenase (Gene Name=nos)

[Back to BioLiP]