Structure of PDB 5liv Chain D

Receptor sequence
>5livD (length=389) Species: 448385 (Sorangium cellulosum So ce56) [Search protein sequence]
DFPLANLFFVPSEDATAFGRRLRAAAQQAPIVFDTAFGMPILLRKSHITT
AYRDTATFSTRMFQAGILNGGLAAMQGDEHARMRRVYNMFFLPRAVSQYE
ERFVRPISEQVVDRLAGKPRVDLLEDFAMELPRRVIGELFGFKLHETDER
VRAMLRGLVRMHDPAAVAESQRAYGETLGLITEVVERESRDTLLGEILRT
LKAEHMDTIEASRQIVLSLILGGYETTSWLVANTIHALLAHPDTLARVRQ
DPSLLPAAIEEGMRWCPSSFGVLRMVERDVRLDDQALSAGTVVCLAGIAG
NYDETAYPSPEVYDIDRKPLPAANVFGGGAHFCVGAPLARMEARVGLQAL
LARFPGLRAVPEERPSFMYGAKDSVAHGPDKLPVLLHHH
3D structure
PDB5liv Structural characterization of CYP260A1 from Sorangium cellulosum to investigate the 1 alpha-hydroxylation of a mineralocorticoid.
ChainD
Resolution2.67 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R210 G279 E282 T283 T284 C390 V391 G392 E399 A433
Catalytic site (residue number reindexed from 1) R156 G222 E225 T226 T227 C333 V334 G335 E342 A376
Enzyme Commision number 1.14.15.19: C-19 steroid 1alpha-hydroxylase.
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 D L123 H131 R135 G279 G280 T283 V329 R331 V382 F383 H388 C390 V391 L72 H80 R84 G222 G223 T226 V272 R274 V325 F326 H331 C333 V334
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

View graph for
Molecular Function
External links
PDB RCSB:5liv, PDBe:5liv, PDBj:5liv
PDBsum5liv
PubMed27878817
UniProtA9FDB7|CP260_SORC5 C-19 steroid 1alpha-hydroxylase (Gene Name=sce1588)

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