Structure of PDB 3fed Chain A

Receptor sequence
>3fedA (length=690) Species: 9606 (Homo sapiens) [Search protein sequence]
SIRWKLVSEMKAENIKSFLRSFTKLPHLAGTEQNFLLAKKIQTQWKKFGL
DSAKLVHYDVLLSYPNETNANYISIVDEHETEIFKTSPPPDGYENVTNIV
PPYNAFSAQGMPEGDLVYVNYARTEDFFKLEREMGINCTGKIVIARYGKI
FRGNKVKNAMLAGAIGIILYSDPADYFAPEVQPYPKGWNLPGTAAQRGNV
LNLNGAGDPLTPGYPAKEYTFRLDVEEGVGIPRIPVHPIGYNDAEILLRY
LGGIAPPDKSWKGALNVSYSIGPGFTGSSFRKVRMHVYNINKITRIYNVV
GTIRGSVEPDRYVILGGHRDSWVFGAIDPTSGVAVLQEIARSFGKLMSKG
WRPRRTIIFASWDAEEFGLLGSTEWAEENVKILQERSIAYINSDSSIEGN
YTLRVDCTPLLYQLVYKLTKEIPSPDDGFESKSLYESWLEKDPSPENKNL
PRINKLGSGSDFEAYFQRLGIASGRARYTKNKKTDKYSSYPVYHTIYETF
ELVEKFYDPTFKKQLSVAQLRGALVYELVDSKIIPFNIQDYAEALKNYAA
SIYNLSKKHDQQLTDHGVSFDSLFSAVKNFSEAASDFHKRLIQVDLNNPI
AVRMMNDQLMLLERAFIDPLGLPGKLFYRHIIFAPSSHNKYAGESFPGIY
DAIFDIENKANSRLAWKEVKKHISIAAFTIQAAAGTLKEV
3D structure
PDB3fed Structural insight into the evolutionary and pharmacologic homology of glutamate carboxypeptidases II and III
ChainA
Resolution1.29 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) H318 D328 E365 E366
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 D328 E366 H494
BS02 ZN A H367 D377 D443 H318 D328 D394
BS03 CA A T259 Y262 E423 E426 T211 Y214 E374 E377
BS04 BIX A R200 N247 D377 E414 E415 G508 R524 R526 Y542 H543 K689 Y690 R152 N199 D328 E365 E366 G459 R475 R477 Y493 H494 K640 Y641 MOAD: Ki=34.6nM
PDBbind-CN: -logKd/Ki=7.46,Ki=34.6nM
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:3fed, PDBe:3fed, PDBj:3fed
PDBsum3fed
PubMed19678840
UniProtQ9Y3Q0|NALD2_HUMAN N-acetylated-alpha-linked acidic dipeptidase 2 (Gene Name=NAALAD2)

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