Structure of PDB 3rbu Chain A

Receptor sequence
>3rbuA (length=691) Species: 9606 (Homo sapiens) [Search protein sequence]
KHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFG
LDSVELAHYDVLLSYPNKTHPNYISIINEDGNEIFNTSLFEPPPPGYENV
SDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIAR
YGKVFRGNKVKNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQ
RGNILNLNGAGDPLTPGYPANEYAYRRGIAEAVGLPSIPVHPIGYYDAQK
LLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTR
IYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGT
LKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLQERGVAYINADS
SIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSP
EFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNKFSGYPLYHSVYET
YELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKYA
DKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDSNPI
VLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIY
DALFDIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA
3D structure
PDB3rbu Efficient and versatile one-step affinity purification of in vivo biotinylated proteins: Expression, characterization and structure analysis of recombinant human glutamate carboxypeptidase II.
ChainA
Resolution1.6 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 D387 E425 H553 D333 E371 H495
BS02 ZN A H377 D387 D453 H323 D333 D399
BS03 CA A T269 Y272 E433 E436 T215 Y218 E379 E382
BS04 G88 A R210 N257 D387 E424 E425 L428 G518 Y552 H553 K699 Y700 R156 N203 D333 E370 E371 L374 G464 Y494 H495 K640 Y641 MOAD: Ki=370pM
PDBbind-CN: -logKd/Ki=9.43,Ki=370pM
BindingDB: Ki=0.280000nM,IC50=300nM,Kd=0.5nM,EC50=0.620000nM
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:3rbu, PDBe:3rbu, PDBj:3rbu
PDBsum3rbu
PubMed22178733
UniProtQ04609|FOLH1_HUMAN Glutamate carboxypeptidase 2 (Gene Name=FOLH1)

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