Structure of PDB 4x3r Chain A

Receptor sequence
>4x3rA (length=690) Species: 9606 (Homo sapiens) [Search protein sequence]
KHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFG
LDSVELAHYDVLLSYPNKTHPNYISIINEDGNEIFNTSLFEPPPPGYENV
SDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIAR
YGKVFRGNKVKNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQ
RGNILNLNGAGDPLTPGYPANEYAYRRGIAEAVGLPSIPVHPIGYYDAQK
LLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTR
IYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGT
LKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLQERGVAYINADS
SIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSP
EFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWETSGYPLYHSVYE
TYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKY
ADKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFNPIV
LRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIYD
ALFDIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA
3D structure
PDB4x3r Design of highly potent urea-based, exosite-binding inhibitors selective for glutamate carboxypeptidase II.
ChainA
Resolution1.86 Å
3D
structure
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Enzymatic activity
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 H377 D387 D453 H323 D333 D399
BS02 ZN A D387 E425 H553 D333 E371 H496
BS03 CA A T269 Y272 E433 E436 T215 Y218 E379 E382
BS04 686 A K207 R210 E424 L428 R463 R511 G518 N519 R536 W541 Y552 H553 K699 Y700 K153 R156 E370 L374 R409 R457 G464 N465 R482 W487 Y495 H496 K639 Y640 MOAD: Ki=0.0086nM
PDBbind-CN: -logKd/Ki=11.07,Ki=8.6pM
BindingDB: Ki=0.008600nM
Gene Ontology
Molecular Function
GO:0004180 carboxypeptidase activity
GO:0004181 metallocarboxypeptidase activity
GO:0008233 peptidase activity
GO:0008237 metallopeptidase activity
GO:0016805 dipeptidase activity
GO:0046872 metal ion binding
GO:1904492 Ac-Asp-Glu binding
GO:1904493 tetrahydrofolyl-poly(glutamate) polymer binding
Biological Process
GO:0006508 proteolysis
GO:0006760 folic acid-containing compound metabolic process
GO:0035609 C-terminal protein deglutamylation
Cellular Component
GO:0005737 cytoplasm
GO:0005886 plasma membrane
GO:0009986 cell surface
GO:0016020 membrane
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4x3r, PDBe:4x3r, PDBj:4x3r
PDBsum4x3r
PubMed25923815
UniProtQ04609|FOLH1_HUMAN Glutamate carboxypeptidase 2 (Gene Name=FOLH1)

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