Structure of PDB 3s7s Chain A

Receptor sequence
>3s7sA (length=452) Species: 9606 (Homo sapiens) [Search protein sequence]
SSIPGPGYCMGIGPLISHGRFLWMGIGSACNYYNRVYGEFMRVWISGEET
LIISKSSSMFHIMKHNHYSSRFGSKLGLQCIGMHEKGIIFNNNPELWKTT
RPFFMKALSGPGLVRMVTVCAESLKTHLDRLEEVTNESGYVDVLTLLRRV
MLDTSNTLFLRIPLDESAIVVKIQGYFDAWQALLIKPDIFFKISWLYKKY
EKSVKDLKDAIEVLIAEKRRRISTEEKLEECMDFATELILAEKRGDLTRE
NVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERD
IKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNI
ILNIGRMHRLEFFPKPNEFTLENFAKNVPYRYFQPFGFGPRGCAGKYIAM
VMMKAILVTLLRRFHVKTLQGQCVESIQKIHDLSLHPDETKNMLEMIFTP
RN
3D structure
PDB3s7s Novel aromatase inhibitors by structure-guided design.
ChainA
Resolution3.21 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) T310 F430 C437
Catalytic site (residue number reindexed from 1) T266 F386 C393
Enzyme Commision number 1.14.14.14: aromatase.
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 A R115 I132 R145 A306 M364 V373 R375 F430 R435 G436 C437 M447 R71 I88 R101 A262 M320 V329 R331 F386 R391 G392 C393 M403
BS02 EXM A R115 I133 W224 D309 L372 V373 M374 L477 R71 I89 W180 D265 L328 V329 M330 L433 BindingDB: Ki=26nM,IC50=900nM
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0008395 steroid hydroxylase activity
GO:0009055 electron transfer activity
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0016712 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
GO:0019825 oxygen binding
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0070330 aromatase activity
Biological Process
GO:0002677 negative regulation of chronic inflammatory response
GO:0006629 lipid metabolic process
GO:0006694 steroid biosynthetic process
GO:0006703 estrogen biosynthetic process
GO:0006710 androgen catabolic process
GO:0006949 syncytium formation
GO:0008209 androgen metabolic process
GO:0008585 female gonad development
GO:0010760 negative regulation of macrophage chemotaxis
GO:0016125 sterol metabolic process
GO:0030540 female genitalia development
GO:0030879 mammary gland development
GO:0032355 response to estradiol
GO:0060065 uterus development
GO:0060736 prostate gland growth
GO:0061370 testosterone biosynthetic process
GO:2000866 positive regulation of estradiol secretion
Cellular Component
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0016020 membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3s7s, PDBe:3s7s, PDBj:3s7s
PDBsum3s7s
PubMed22951074
UniProtP11511|CP19A_HUMAN Aromatase (Gene Name=CYP19A1)

[Back to BioLiP]