Structure of PDB 2e2l Chain F

Receptor sequence
>2e2lF (length=317) Species: 85962 (Helicobacter pylori 26695) [Search protein sequence]
GFLVAAIQFPVPIVNSRKDIDHNIESIIRTLHATKAGYPGVELIIFPEYS
TQGLNTAKWLSEEFLLDVPGKETELYAKACKEAKVYGVFSIMERNPDSNK
NPYNTAIIIDPQGEIILKYRKLFPWNPIEPWYPGDLGMPVCEGPGGSKLA
VCISHDGMIPELAREAAYKGCNVYIRISGYSTQVNDQWILTNRSNAWHNL
MYTVSVNLAGYYFGEGQICNFDGTTLVQGHRNPWEIVTGEIYPKMADNAR
LSWGLENNIYNLGHRGYVAKPGGEHDAGLTYIKDLAAGKYKLPWEDHMKI
KDGSIYGYPTTGGRFGK
3D structure
PDB2e2l Crystal structure of Helicobacter pylori formamidase AmiF reveals a cysteine-glutamate-lysine catalytic triad
ChainF
Resolution2.29 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E60 N116 D122 P139 S166 Y192
Catalytic site (residue number reindexed from 1) E48 N104 D110 P127 S154 Y180
Enzyme Commision number 3.5.1.49: formamidase.
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 ARF F E60 W137 S166 H167 Y192 E48 W125 S154 H155 Y180
Gene Ontology
Molecular Function
GO:0004328 formamidase activity
GO:0016787 hydrolase activity
GO:0050126 N-carbamoylputrescine amidase activity
Biological Process
GO:0033388 putrescine biosynthetic process from arginine

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Molecular Function
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Biological Process
External links
PDB RCSB:2e2l, PDBe:2e2l, PDBj:2e2l
PDBsum2e2l
PubMed17307742
UniProtO25836|AMIF_HELPY Formamidase (Gene Name=amiF)

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