Structure of PDB 7yh4 Chain A

Receptor sequence
>7yh4A (length=400) Species: 9606 (Homo sapiens) [Search protein sequence]
LYFQGSLELLKLRSAECIDEAAERLGALSRAIWSQPELAYEEHHAHRVLT
HFFEREPPAASWAVQPHYQLPTAFRAEWEPPEARPRPLHLGFLCEYDALP
GIGHACGHNLIAEVGAAAALGVRGALEGLPRPPPPVKVVVLGTPAEEDGG
GKIDLIEAGAFTNLDVVFMAHPSQENAAYLPDMAEHDVTVKYYGKASHSA
SYPWEGLNALDAAVLAYNNLSVFRQQMKPTWRVHGIIKNGGVKPNIIPSY
SELIYYFRAPSMKELQVLTKKAEDCFRAAALASGCTVEIKGGAHDYYNVL
PNKSLWKAYMENGRKLGIEFIGSTDFGNVSFVVPGIHPYFHIGSNALNHT
EQYTEAAGSQEAQFYTLRTAKALAMTALDVIFKPELLEGIREDFKLKLQE
3D structure
PDB7yh4 Crystal structure of human cytosolic beta-alanyl lysine dipeptidase (PM20D2)
ChainA
Resolution2.03 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 3.4.13.4: Xaa-Arg dipeptidase.
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 C124 E165 H377 C106 E147 H349
BS02 ZN A H126 H189 H108 H171
Gene Ontology
Molecular Function
GO:0004180 carboxypeptidase activity
GO:0005515 protein binding
GO:0016787 hydrolase activity
GO:0016805 dipeptidase activity
GO:0042802 identical protein binding
GO:0071713 para-aminobenzoyl-glutamate hydrolase activity
Biological Process
GO:0006508 proteolysis
GO:0046657 folic acid catabolic process
GO:0051246 regulation of protein metabolic process
Cellular Component
GO:0005654 nucleoplasm
GO:0005737 cytoplasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:7yh4, PDBe:7yh4, PDBj:7yh4
PDBsum7yh4
PubMed
UniProtQ8IYS1|P20D2_HUMAN Xaa-Arg dipeptidase (Gene Name=PM20D2)

[Back to BioLiP]