Structure of PDB 5bv5 Chain B

Receptor sequence
>5bv5B (length=288) Species: 2287 (Saccharolobus solfataricus) [Search protein sequence]
MYDWFSEMRKKDPVYYDGNIWQVFSYRYTKEVLNNFSKFSSDFSPQKLQT
LETFIRETTRSLLDSIDPREDDIVKKLAVPLPIIVISKILGLPIKEKFKE
WSDLLGKKYLELIGYVKLSDIEKLGYIILLLIAGNEATTNLISNSVIDFT
RFNLWQRIREENLYLKAIEEALRYSPPVMRTVRKTKERVKLGDQTIEEGE
YVRVWIASANRDEEVFHDGEKFIPDRNPNPHLSFGSGILHLGAPLARLEA
RIAIEEFSKRFRHIEILDTEKVPNEVLNGYKRLVVRLK
3D structure
PDB5bv5 Structural Adaptability Facilitates Histidine Heme Ligation in a Cytochrome P450.
ChainB
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) A133 E136 A137 T138 H240 L241 G242 E249 L277
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 B L207 G210 A213 V254 T257 R259 S309 F310 G311 H317 L131 G134 A137 V178 T181 R183 S233 F234 G235 H240
BS02 PIM B A213 L354 A137 L277
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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