Structure of PDB 2flq Chain A

Receptor sequence
>2flqA (length=359) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
RQHDEQLMTKAEQFIIASYRELGKSEQEIKRRVNEIRWEVEQTGTYRHTY
EELSYGAKMAWRHSNRCIGRLFWQSLHVIDAREAVTEEEVFSYLFHHIEV
ATNGGKIRPTITIFRPNGEVRIWNHQLIRYAGYETEEGIIGDSSSLTFTR
ACEQLGWKGEKTPFDVLPLVIQVGGQKPVWTPIPKELVLEVPIEHPEFPW
FRDLQLKWYAVPIISDMCLEIGGIRYMAAPFNGWYMGTEIGARNFADDYR
YNMLPKVASCMGLDTNSNASLWKDKALVELNIAVLYSYKKAGVSIVDHHT
AARQFQLFEQQEKAAGRHVTGDWTWLIPPLSPATTHIFHRSYDNTMMLPN
FFYQDRPYE
3D structure
PDB2flq Structure and Reactivity of a Thermostable Prokaryotic Nitric-oxide Synthase That Forms a Long-lived Oxy-Heme Complex.
ChainA
Resolution3.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C76 R79 W243 E248
Catalytic site (residue number reindexed from 1) C67 R70 W234 E239
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 ARG A Q135 P221 I223 W243 Y244 E248 N253 Q126 P212 I214 W234 Y235 E239 N244
BS02 HEM A W70 C76 F240 N241 G242 W243 W334 F360 Y362 W61 C67 F231 N232 G233 W234 W325 F351 Y353
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:2flq, PDBe:2flq, PDBj:2flq
PDBsum2flq
PubMed16407211
UniProtQ5KZC5

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