Structure of PDB 4fdh Chain L

Receptor sequence
>4fdhL (length=456) Species: 9606 (Homo sapiens) [Search protein sequence]
LPFEAMPQHPGNRWLRLLQIWREQGYEHLHLEMHQTFQELGPIFRYPRMV
CVMLPEDVEKLQQVDSLHPCRMILEPWVAYRQHRGHKCGVFLLNGPEWRF
NRLRLNPDVLSPKAVQRFLPMVDAVARDFSQALKKKVLQNARGSLTLDVQ
PSIFHYTIEASNLALFGERLGLVGHSPSSASLNFLHALEVMFKSTVQLMF
MPRSLSRWISPKVWKEHFEAWDCIFQYGDNCIQKIYQELAFNRPQHYTGI
VAELLLKAELSLEAIKANSMELTAGSVDTTAFPLLMTLFELARNPDVQQI
LRQESLAAAASISEHPQKATTELPLLRAALKETLRLYPVGLFLERVVSSD
LVLQNYHIPAGTLVQVFLYSLGRNAALFPRPERYNPQRWLDFHHVPFGFG
MRQCLGRRLAEAEMLLLLHHVLKHFLVETLTQEDIKMVYSFILRPGTSPL
LTFRAI
3D structure
PDB4fdh Structural insights into aldosterone synthase substrate specificity and targeted inhibition.
ChainL
Resolution2.71 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) T318 F443 C450
Catalytic site (residue number reindexed from 1) T279 F397 C404
Enzyme Commision number 1.14.15.4: steroid 11beta-monooxygenase.
1.14.15.5: corticosterone 18-monooxygenase.
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 L R110 V129 F130 W137 R141 L311 S315 T318 V378 R384 P442 F443 R448 C450 G452 A456 R71 V90 F91 W98 R102 L272 S276 T279 V339 R345 P396 F397 R402 C404 G406 A410
BS02 0T3 L W116 F130 E310 G314 T318 W77 F91 E271 G275 T279 BindingDB: IC50=1nM
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0004507 steroid 11-beta-monooxygenase activity
GO:0005506 iron ion binding
GO:0008395 steroid hydroxylase activity
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:0047783 corticosterone 18-monooxygenase activity
Biological Process
GO:0002017 regulation of blood volume by renal aldosterone
GO:0003091 renal water homeostasis
GO:0006629 lipid metabolic process
GO:0006694 steroid biosynthetic process
GO:0006700 C21-steroid hormone biosynthetic process
GO:0006704 glucocorticoid biosynthetic process
GO:0006705 mineralocorticoid biosynthetic process
GO:0008203 cholesterol metabolic process
GO:0016125 sterol metabolic process
GO:0032342 aldosterone biosynthetic process
GO:0032870 cellular response to hormone stimulus
GO:0034650 cortisol metabolic process
GO:0034651 cortisol biosynthetic process
GO:0035865 cellular response to potassium ion
GO:0055075 potassium ion homeostasis
GO:0055078 sodium ion homeostasis
GO:0071375 cellular response to peptide hormone stimulus
GO:1901615 organic hydroxy compound metabolic process
Cellular Component
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4fdh, PDBe:4fdh, PDBj:4fdh
PDBsum4fdh
PubMed23322723
UniProtP19099|C11B2_HUMAN Cytochrome P450 11B2, mitochondrial (Gene Name=CYP11B2)

[Back to BioLiP]