Structure of PDB 1xfu Chain E Binding Site BS01

Receptor Information
>1xfu Chain E (length=735) Species: 1392 (Bacillus anthracis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NNLVKTEFTNETLDKIQQTQDLLKKIPKDVLEIYSELGGEIYFTDIDLVE
HKELQDLSEEEKNSMNSRGEKVPFASRFVFEKKRETPKLIINIKDYAINS
EQSKEVYYEIGKGISLDIISKDKSLDPEFLNLIKSLSDDSDSSDLLFSQK
FKEKLELNNKSIDINFIKENLTEFQHAFSLAFSYYFAPDHRTVLELYAPD
MFEYMNKLEKGGFEKISESLKKEGVEKDRIDVLKGEKALKASGLVPEHAD
AFKKIARELNTYILFRPVNKLATNLIKSGVATKGLNVHGKSSDWGPVAGY
IPFDQDLSKKHGQQLAVEKGNLENKKSITEHEGEIGKIPLKLDHLRIEEL
KENGIILKGKKEIDNGKKYYLLESNNQVYEFRISDENNEVQYKTKEGKIT
VLGEKFNWRNIEVMAKNVEGVLKPLTADYDLFALAPSLTEIKKQIPQKEW
DKVVNTPNSLEKQKGVTNLLIKYGIERKPDSTKGTLSNWQKQMLDRLNEA
VKYTGYTGGDVVNHGTEQDNEEFPEKDNEIFIINPEGEFILTKNWEMTGR
FIEKNITGKDYLYYFNRSYNKIAPGNKAYIEWTDPITKAKINTIPTSAEF
IKNLSSIRRSSNVGVYKDSGDKDEFAKKESVKKIAGYLSDYYNSANHIFS
QEKKRKISIFRGIQAYNEIENVLKSKQIAPEYKNYFQYLKERITNQVQLL
LTHQKSNIEFKLLYKQLNFTENETDNFEVFQKIID
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain1xfu Chain E Residue 904 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1xfu Calcium-independent calmodulin binding and two-metal-ion catalytic mechanism of anthrax edema factor.
Resolution3.35 Å
Binding residue
(original residue number in PDB)		D491 D493 H577
Binding residue
(residue number reindexed from 1)		D428 D430 H514
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y626 Y627 R630 Y679 D686
Catalytic site (residue number reindexed from 1) Y563 Y564 R567 Y616 D623
Enzyme Commision number 4.6.1.1: adenylate cyclase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004016 adenylate cyclase activity
GO:0005515 protein binding
GO:0005516 calmodulin binding
GO:0005524 ATP binding
GO:0008237 metallopeptidase activity
GO:0008294 calcium- and calmodulin-responsive adenylate cyclase activity
GO:0010856 adenylate cyclase activator activity
GO:0016829 lyase activity
GO:0036094 small molecule binding
GO:0046872 metal ion binding
GO:0090729 toxin activity
Biological Process
GO:0006171 cAMP biosynthetic process
GO:0052027 symbiont-mediated perturbation of host signal transduction pathway
Cellular Component
GO:0005576 extracellular region
GO:0030430 host cell cytoplasm
GO:0044164 host cell cytosol
GO:1902494 catalytic complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1xfu, PDBe:1xfu, PDBj:1xfu
PDBsum1xfu
PubMed15719022
UniProtP40136|CYAA_BACAN Calmodulin-sensitive adenylate cyclase (Gene Name=cya)

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