Structure of PDB 3fee Chain A

Receptor sequence
>3feeA (length=689) Species: 9606 (Homo sapiens) [Search protein sequence]
SIRWKLVSEMKAENIKSFLRSFTKLPHLAGTEQNFLLAKKIQTQWKKFGL
DSAKLVHYDVLLSYPNETNANYISIVDEHETEIFKTSLEPPPDGYENVTN
IVPPYNAFSAQGMPEGDLVYVNYARTEDFFKLEREMGINCTGKIVIARYG
KIFRGNKVKNAMLAGAIGIILYSDPADYFAPEVQPYPKGWNLPGTAAQRG
NVLNLNGAGDPLTPGYPAKEYTFRLDVEEGVGIPRIPVHPIGYNDAEILL
RYLGGIAPPDKSWKGALNVSYSIGPGFTGSSFRKVRMHVYNINKITRIYN
VVGTIRGSVEPDRYVILGGHRDSWVFGAIDPTSGVAVLQEIARSFGKLMS
KGWRPRRTIIFASWDAEEFGLLGSTEWAEENVKILQERSIAYINSDSSIE
GNYTLRVDCTPLLYQLVYKLTKEIPSPDDGFESKSLYESWLEKDPSPENK
NLPRINKLGSGSDFEAYFQRLGIASGRARYTKNDKYSSYPVYHTIYETFE
LVEKFYDPTFKKQLSVAQLRGALVYELVDSKIIPFNIQDYAEALKNYAAS
IYNLSKKHDQQLTDHGVSFDSLFSAVKNFSEAASDFHKRLIQVDLNNPIA
VRMMNDQLMLLERAFIDPLGLPGKLFYRHIIFAPSSHNKYAGESFPGIYD
AIFDIENKANSRLAWKEVKKHISIAAFTIQAAAGTLKEV
3D structure
PDB3fee Structural insight into the evolutionary and pharmacologic homology of glutamate carboxypeptidases II and III
ChainA
Resolution1.56 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H367 D377 E414 E415
Catalytic site (residue number reindexed from 1) H320 D330 E367 E368
Enzyme Commision number 3.4.17.21: glutamate carboxypeptidase II.
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 ZN A D377 E415 H543 D330 E368 H493
BS02 ZN A H367 D377 D443 H320 D330 D396
BS03 CA A T259 Y262 E423 E426 T213 Y216 E376 E379
BS04 QUS A R200 N247 E414 G508 Y542 K689 Y690 R154 N201 E367 G461 Y492 K639 Y640 MOAD: Ki=230nM
PDBbind-CN: -logKd/Ki=6.64,Ki=230nM
Gene Ontology
Molecular Function
GO:0004180 carboxypeptidase activity
GO:0004181 metallocarboxypeptidase activity
GO:0005515 protein binding
GO:0008236 serine-type peptidase activity
GO:0008237 metallopeptidase activity
GO:0008239 dipeptidyl-peptidase activity
GO:0016805 dipeptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0005886 plasma membrane
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3fee, PDBe:3fee, PDBj:3fee
PDBsum3fee
PubMed19678840
UniProtQ9Y3Q0|NALD2_HUMAN N-acetylated-alpha-linked acidic dipeptidase 2 (Gene Name=NAALAD2)

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