Structure of PDB 3fmq Chain B

Receptor sequence

>3fmqB (length=356) Species: 6035 (Encephalitozoon cuniculi)

CILLNQAEELPIEFLPKDGVYGKGKLFDSRNMEIENFTESDILQDARRAA
EAHRRARYRVQSIVRPGITLLEIVRSIEDSTRTLLKGERNNGIGFPAGMS
MNSCAAHYTVNPGEQDIVLKEDDVLKIDFGTHSDGRIMDSAFTVAFKENL
EPLLVAAREGTETGIKSLGVDVRVCDIGRDINEVISSYEVEIGGRMWPIR
PISDLHGHSISQFRIHGGISIPAVNNRDTTRIKGDSFYAVETFATTGKGS
IDDRPPCSHFVLNTYKSRKLFNKDLIKVYEFVKDSLGTLPFSPRHLDYYG
LVKGGSLKSVNLLTMMGLLTPYPPLNDIDGCKVAQFEHTVYLSEHGKEVL
TRGDDY

3D structure

• PDB: 3fmq Structure of a microsporidian methionine aminopeptidase type 2 complexed with fumagillin and TNP-470.
• Chain: B
• Resolution: 2.5 Å

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	B	D141 H210 E243 E339	D139 H208 E241 E337
BS02	FE	B	D130 D141 E339	D128 D139 E337
BS03	FUG	B	F97 H109 L207 H208 H210 E243 Y324	F95 H107 L205 H206 H208 E241 Y322

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

External links

• PDB: RCSB:3fmq, PDBe:3fmq, PDBj:3fmq
• PDBsum: 3fmq
• PubMed: 19660503
• UniProt: Q8SR45|MAP2_ENCCU Methionine aminopeptidase 2 (Gene Name=MAP2)