Structure of PDB 3fm3 Chain B Binding Site BS01
Receptor Information
>3fm3 Chain B (length=356) Species:
6035
(Encephalitozoon cuniculi) [
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CILLNQAEELPIEFLPKDGVYGKGKLFDSRNMEIENFTESDILQDARRAA
EAHRRARYRVQSIVRPGITLLEIVRSIEDSTRTLLKGERNNGIGFPAGMS
MNSCAAHYTVNPGEQDIVLKEDDVLKIDFGTHSDGRIMDSAFTVAFKENL
EPLLVAAREGTETGIKSLGVDVRVCDIGRDINEVISSYEVEIGGRMWPIR
PISDLHGHSISQFRIHGGISIPAVNNRDTTRIKGDSFYAVETFATTGKGS
IDDRPPCSHFVLNTYKSRKLFNKDLIKVYEFVKDSLGTLPFSPRHLDYYG
LVKGGSLKSVNLLTMMGLLTPYPPLNDIDGCKVAQFEHTVYLSEHGKEVL
TRGDDY
Ligand information
Ligand ID
FE
InChI
InChI=1S/Fe/q+3
InChIKey
VTLYFUHAOXGGBS-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0
[Fe+3]
Formula
Fe
Name
FE (III) ION
ChEMBL
DrugBank
DB13949
ZINC
PDB chain
3fm3 Chain B Residue 551 [
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Receptor-Ligand Complex Structure
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PDB
3fm3
Structure of a microsporidian methionine aminopeptidase type 2 complexed with fumagillin and TNP-470.
Resolution
2.18 Å
Binding residue
(original residue number in PDB)
D141 H210 E243 E339
Binding residue
(residue number reindexed from 1)
D139 H208 E241 E337
Annotation score
4
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.
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:3fm3
,
PDBe:3fm3
,
PDBj:3fm3
PDBsum
3fm3
PubMed
19660503
UniProt
Q8SR45
|MAP2_ENCCU Methionine aminopeptidase 2 (Gene Name=MAP2)
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