Structure of PDB 4fxq Chain A

Receptor sequence

>4fxqA (length=445) Species: 1396 (Bacillus cereus)

ENSKKTQELVEKLPHEVLELYKNVGGEIYITDKRLTQHEELSDSSHKDMF
IVSSEGKSFPLREHFVFAKGGKEPSLIIHAEDYASHLSSVEVYYELGKAI
IRDTFPLNQKELGNPKFINAINEVNQQKEGKGVNAKADEDGRDLLFGKEL
KKNLEHGQLVDLDLISGNLSEFQHVFAKSFALYYEPHYKEALKSYAPALF
NYMLELDQMRFKEISDDVKEKNKNVLDFKWYTRKAESWGVQTFKNWKENL
TISEKDIITGYTGSKYDPINEYLRKYDGEIIPNIGGDLDKKSKKALEKIE
NQIKNLDAALQKSKITENLIVYRRVSELQFGKKYEDYNLRQNGIINEEKV
MELESNFKGQTFIQHNYMSTSLVQDPHQSYSNDRYPILLEITIPEGVHGA
YIADMSEYPGQYEMLINRGYTFKYDKFSIVKPGKEYLKVNLSIYL

3D structure

• PDB: 4fxq Certhrax Toxin, an Anthrax-related ADP-ribosyltransferase from Bacillus cereus.
• Chain: A
• Resolution: 1.9599 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): S387 E431
• Catalytic site (residue number reindexed from 1): S369 E413
• Enzyme Commision number: 2.4.2.-

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	G9L	A	G281 Y284 R341 R342 S387 T388 S389 Y398 Q429 E431	G263 Y266 R323 R324 S369 T370 S371 Y380 Q411 E413	MOAD: Kd=1.7uM PDBbind-CN: -logKd/Ki=5.77,Kd=1.7uM

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0003824 catalytic activity
• GO:0008237 metallopeptidase activity
• GO:0016757 glycosyltransferase activity
• GO:0016779 nucleotidyltransferase activity
• GO:0046872 metal ion binding
• GO:0090729 toxin activity

Biological Process

• GO:0035821 modulation of process of another organism

Cellular Component

• GO:0005576 extracellular region

External links

• PDB: RCSB:4fxq, PDBe:4fxq, PDBj:4fxq
• PDBsum: 4fxq
• PubMed: 22992735
• UniProt: Q4MV79|CRAX_BACCE Putative ADP-ribosyltransferase Certhrax (Gene Name=BCE_G9241_pBC218_0027)