Structure of PDB 5bv5 Chain C

Receptor sequence
>5bv5C (length=311) Species: 2287 (Saccharolobus solfataricus) [Search protein sequence]
MYDWFSEMRKKDPVYYDGNIWQVFSYRYTKEVLNNFSKFSSDLPLHDELR
SMSADIFSPQKLQTLETFIRETTRSLLDSIDPREDDIVKKLAVPLPIIVI
SKILGLPGEIFELGKKYLELIGYVKDHLNSGTEVVSRVVNLSDIEKLGYI
ILLLIAGNEATTNLISNSVIDFTRFNLWQRIREENLYLKAIEEALRYSPP
VMRTVRKTKERVKLGDQTIEEGEYVRVWIASANRDEEVFHDGEKFIPDRN
PNPHLSFGSGIHLHLGAPLARLEARIAIEEFSKRFRHIEILDTEKVPNEV
LNGYKRLVVRL
3D structure
PDB5bv5 Structural Adaptability Facilitates Histidine Heme Ligation in a Cytochrome P450.
ChainC
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) A156 E159 A160 T161 H264 L265 G266 E273 L301
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 C H76 G210 N211 A213 V254 R259 S309 F310 G311 H317 H46 G157 N158 A160 V201 R206 S256 F257 G258 H264
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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