Structure of PDB 4fdh Chain G
Receptor sequence
>4fdhG (length=463) Species:
9606
(Homo sapiens) [
Search protein sequence
]
TVLPFEAMPQHPGNRWLRLLQIWREQGYEHLHLEMHQTFQELGPIFRYNL
GGPRMVCVMLPEDVEKLQQVDSLHPCRMILEPWVAYRQHRGHKCGVFLLN
GPEWRFNRLRLNPDVLSPKAVQRFLPMVDAVARDFSQALKKKVLQNARGS
LTLDVQPSIFHYTIEASNLALFGERLGLVGHSPSSASLNFLHALEVMFKS
TVQLMFMPRSLSRWISPKVWKEHFEAWDCIFQYGDNCIQKIYQELAFNRP
QHYTGIVAELLLKAELSLEAIKANSMELTAGSVDTTAFPLLMTLFELARN
PDVQQILRQESLAAAASISEHPQKATTELPLLRAALKETLRLYPVGLFLE
RVVSSDLVLQNYHIPAGTLVQVFLYSLGRNAALFPRPERYNPQRWLDNFH
HVPFGFGMRQCLGRRLAEAEMLLLLHHVLKHFLVETLTQEDIKMVYSFIL
RPGTSPLLTFRAI
3D structure
PDB
4fdh
Structural insights into aldosterone synthase substrate specificity and targeted inhibition.
Chain
G
Resolution
2.71 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)
T285 F404 C411
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
G
R110 V129 F130 W137 R141 L311 S315 T318 R384 P442 F443 G444 R448 Q449 C450 G452 A456
R77 V96 F97 W104 R108 L278 S282 T285 R351 P403 F404 G405 R409 Q410 C411 G413 A417
BS02
0T3
G
W116 F130 E310 A313 G314 T318 I488
W83 F97 E277 A280 G281 T285 I449
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
PDBsum
4fdh
PubMed
23322723
UniProt
P19099
|C11B2_HUMAN Cytochrome P450 11B2, mitochondrial (Gene Name=CYP11B2)
[
Back to BioLiP
]