Structure of PDB 5bv5 Chain A

Receptor sequence
>5bv5A (length=315) Species: 2287 (Saccharolobus solfataricus) [Search protein sequence]
MYDWFSEMRKKDPVYYDGNIWQVFSYRYTKEVLNNFSKFSSDLPPLHDEL
RSMSADIFSPQKLQTLETFIRETTRSLLDSIDPREDDIVKKLAVPLPIIV
ISKILGLPIEDKEKFKEWSIFELGKKYLELIGYVKDHLSGTEVVSRLSDI
EKLGYIILLLIAGNEATTNLISNSVIDFTRFNLWQRIREENLYLKAIEEA
LRYSPPVMRTVRKTKERVKLGDQTIEEGEYVRVWIASANRDEEVFHDGEK
FIPDRNPNPHLSFGSLHLGAPLARLEARIAIEEFSKRFRHIEILDTEKVP
NEVLNGYKRLVVRLK
3D structure
PDB5bv5 Structural Adaptability Facilitates Histidine Heme Ligation in a Cytochrome P450.
ChainA
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A209 E212 A213 T214 H317 L318 G319 E326 L354
Catalytic site (residue number reindexed from 1) A162 E165 A166 T167 H267 L268 G269 E276 L304
Enzyme Commision number 1.11.1.7: peroxidase.
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 L207 G210 A213 T214 L217 P253 V254 R259 S309 F310 S312 H317 L160 G163 A166 T167 L170 P206 V207 R212 S262 F263 S265 H267
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0004601 peroxidase 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
GO:0140825 lactoperoxidase activity
Biological Process
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5bv5, PDBe:5bv5, PDBj:5bv5
PDBsum5bv5
PubMed26299431
UniProtQ55080|CP119_SULAC Cytochrome P450 119 (Gene Name=cyp119)

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