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3FMQ

Crystal structure of an Encephalitozoon cuniculi methionine aminopeptidase type 2 with angiogenesis inhibitor fumagillin bound

Replaces:  3CMK
Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0004239molecular_functioninitiator methionyl aminopeptidase activity
A0005737cellular_componentcytoplasm
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008235molecular_functionmetalloexopeptidase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0070006molecular_functionmetalloaminopeptidase activity
B0004177molecular_functionaminopeptidase activity
B0004239molecular_functioninitiator methionyl aminopeptidase activity
B0005737cellular_componentcytoplasm
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008235molecular_functionmetalloexopeptidase activity
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
B0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE A 451
ChainResidue
AASP141
AHIS210
AGLU243
AGLU339
AFE452
AFUG481

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 452
ChainResidue
AGLU339
AFE451
AASP130
AASP141
AGLU243

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FUG A 481
ChainResidue
AHIS109
AASP206
ALEU207
AHIS208
AILE217
AHIS218
ATYR324
AFE451

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
AARG77
AARG296

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
ALYS88
AHOH605
BARG77
BARG296

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE B 451
ChainResidue
BASP141
BHIS210
BGLU243
BGLU339
BFE452
BFUG481

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE B 452
ChainResidue
BASP130
BASP141
BGLU339
BFE451

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FUG B 481
ChainResidue
BHIS109
BASP206
BLEU207
BHIS208
BHIS218
BGLU243
BTYR324
BFE451

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 503
ChainResidue
ALYS305
BARG91
BPHE215
BHOH598
BHOH677

Functional Information from PROSITE/UniProt
site_idPS01202
Number of Residues17
DetailsMAP_2 Methionine aminopeptidase subfamily 2 signature. DVlKIDfGtHSDGrimD
ChainResidueDetails
AASP125-ASP141

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03175","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19660503","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AILE221
AGLU243

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
BILE221
BGLU243

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AGLU243

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
BGLU243

245663

PDB entries from 2025-12-03

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