Structure of PDB 3b4x Chain A

Receptor sequence
>3b4xA (length=367) Species: 111955 (Sulfurisphaera tokodaii) [Search protein sequence]
MYDWFKQMRKESPVYYDGKVWNLFKYEDCKMVLNDHKRFSSNLTGYNDKL
EMLRSGKVFFDIPTRYTMLTSDPPLHDELRNLTADAFNPSNLPVDFVREV
TVKLLSELDEEFDVIESFAIPLPILVISKMLGINPDVKKVKDWSDLVALR
LGRADEIFSIGRKYLELISFSKKELDSRKGKEIVDLTGKIANSNLSELEK
EGYFILLMIAGNETTTNLIGNAIEDFTLYNSWDYVREKGALKAVEEALRF
SPPVMRTIRVTKEKVKIRDQVIDEGELVRVWIASANRDEEVFKDPDSFIP
DRTPNPHLSFGSGIHLCLGAPLARLEARIALEEFAKKFRVKEIVKKEKID
NEVLNGYRKLVVRVERT
3D structure
PDB3b4x Monooxygenation by Thermophilic Cytochrome P450 via Direct Electron Transfer from NADH without Redox Partner
ChainA
Resolution1.94 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A210 E213 T214 T215 C317 E326 L354
Catalytic site (residue number reindexed from 1) A210 E213 T214 T215 C317 E326 L354
Enzyme Commision number 1.14.-.-
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 M68 L69 H76 A210 G211 T214 T215 P253 T257 R259 S309 F310 H315 C317 L318 G319 M68 L69 H76 A210 G211 T214 T215 P253 T257 R259 S309 F310 H315 C317 L318 G319
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0020037 heme binding
GO:0046872 metal ion binding
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Cellular Component
External links
PDB RCSB:3b4x, PDBe:3b4x, PDBj:3b4x
PDBsum3b4x
PubMed
UniProtQ972I2|CP119_SULTO Cytochrome P450 119 (Gene Name=cyp119)

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