Structure of PDB 1y0v Chain E

Receptor sequence
>1y0vE (length=735) Species: 1392 (Bacillus anthracis) [Search protein sequence]
NNLVKTEFTNETLDKIQQTQDLLKKIPKDVLEIYSELGGEIYFTDIDLVE
HKELQDLSEEEKNSMNSRGEKVPFASRFVFEKKRETPKLIINIKDYAINS
EQSKEVYYEIGKGISLDIISKDKSLDPEFLNLIKSLSDDSDSSDLLFSQK
FKEKLELNNKSIDINFIKENLTEFQHAFSLAFSYYFAPDHRTVLELYAPD
MFEYMNKLEKGGFEKISESLKKEGVEKDRIDVLKGEKALKASGLVPEHAD
AFKKIARELNTYILFRPVNKLATNLIKSGVATKGLNVHGKSSDWGPVAGY
IPFDQDLSKKHGQQLAVEKGNLENKKSITEHEGEIGKIPLKLDHLRIEEL
KENGIILKGKKEIDNGKKYYLLESNNQVYEFRISDENNEVQYKTKEGKIT
VLGEKFNWRNIEVMAKNVEGVLKPLTADYDLFALAPSLTEIKKQIPQKEW
DKVVNTPNSLEKQKGVTNLLIKYGIERKPDSTKGTLSNWQKQMLDRLNEA
VKYTGYTGGDVVNHGTEQDNEEFPEKDNEIFIINPEGEFILTKNWEMTGR
FIEKNITGKDYLYYFNRSYNKIAPGNKAYIEWTDPITKAKINTIPTSAEF
IKNLSSIRRSSNVGVYKDSGDKDEFAKKESVKKIAGYLSDYYNSANHIFS
QEKKRKISIFRGIQAYNEIENVLKSKQIAPEYKNYFQYLKERITNQVQLL
LTHQKSNIEFKLLYKQLNFTENETDNFEVFQKIID
3D structure
PDB1y0v Calcium-independent calmodulin binding and two-metal-ion catalytic mechanism of anthrax edema factor
ChainE
Resolution3.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 MG E D491 D493 H577 D428 D430 H514
BS02 POP E K346 S354 K372 K283 S291 K309
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008237 metallopeptidase activity
GO:0008294 calcium- and calmodulin-responsive adenylate cyclase activity
GO:0046872 metal ion binding
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Cellular Component
External links
PDB RCSB:1y0v, PDBe:1y0v, PDBj:1y0v
PDBsum1y0v
PubMed15719022
UniProtP40136|CYAA_BACAN Calmodulin-sensitive adenylate cyclase (Gene Name=cya)

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