Structure of PDB 3fmr Chain A

Receptor sequence
>3fmrA (length=356) Species: 6035 (Encephalitozoon cuniculi) [Search protein sequence]
CILLNQAEELPIEFLPKDGVYGKGKLFDSRNMEIENFTESDILQDARRAA
EAHRRARYRVQSIVRPGITLLEIVRSIEDSTRTLLKGERNNGIGFPAGMS
MNSCAAHYTVNPGEQDIVLKEDDVLKIDFGTHSDGRIMDSAFTVAFKENL
EPLLVAAREGTETGIKSLGVDVRVCDIGRDINEVISSYEVEIGGRMWPIR
PISDLHGHSISQFRIHGGISIPAVNNRDTTRIKGDSFYAVETFATTGKGS
IDDRPPCSHFVLNTYKSRKLFNKDLIKVYEFVKDSLGTLPFSPRHLDYYG
LVKGGSLKSVNLLTMMGLLTPYPPLNDIDGCKVAQFEHTVYLSEHGKEVL
TRGDDY
3D structure
PDB3fmr Structure of a microsporidian methionine aminopeptidase type 2 complexed with fumagillin and TNP-470.
ChainA
Resolution2.89 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D130 D141 H210 H218 E243 E339
Catalytic site (residue number reindexed from 1) D128 D139 H208 H216 E241 E337
Enzyme Commision number 3.4.11.18: methionyl aminopeptidase.
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 FE A D141 H210 E243 E339 D139 H208 E241 E337
BS02 FE A D130 D141 E339 D128 D139 E337
BS03 TN4 A F97 H109 D206 L207 H208 H218 Y324 F95 H107 D204 L205 H206 H216 Y322 PDBbind-CN: -logKd/Ki=7.97,IC50=10.6nM
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0004239 initiator methionyl aminopeptidase activity
GO:0008235 metalloexopeptidase activity
GO:0046872 metal ion binding
GO:0070006 metalloaminopeptidase activity
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3fmr, PDBe:3fmr, PDBj:3fmr
PDBsum3fmr
PubMed19660503
UniProtQ8SR45|MAP2_ENCCU Methionine aminopeptidase 2 (Gene Name=MAP2)

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