Structure of PDB 1wy2 Chain B Binding Site BS02
Receptor Information
>1wy2 Chain B (length=347) Species:
70601
(Pyrococcus horikoshii OT3) [
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NEKVKKIIEFMDKNSIDAVLIAKNPNVYYISGASPLAGGYILITGESATL
YVPELEYEMAKEESNIPVEKFKKMDEFYKALEGIKSLGIESSLPYGFIEE
LKKKANIKEFKKVDDVIRDMRIIKSEKEIKIIEKACEIADKAVMAAIEEI
TEGKKEREVAAKVEYLMKMNGAEKPAFDTIIASGYRSALPHGVASDKRIE
RGDLVVIDLGALYQHYNSDITRTIVVGSPNEKQKEIYEIVLEAQKKAVES
AKPGITAKELDSIARNIIAEYGYGEYFNHSLGHGVGLEVHEWPRVSQYDE
TVLREGMVITIEPGIYIPKIGGVRIEDTILITKNGSKRLTKTERELI
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
1wy2 Chain B Residue 408 [
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Receptor-Ligand Complex Structure
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PDB
1wy2
Crystal Structure of the Prolidase from Pyrococcus horikoshii OT3
Resolution
1.7 Å
Binding residue
(original residue number in PDB)
D223 H287 E316 E330
Binding residue
(residue number reindexed from 1)
D219 H283 E312 E326
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
H195 D212 D223 T225 H283 H287 H294 E316 Y320 R328 E330
Catalytic site (residue number reindexed from 1)
H191 D208 D219 T221 H279 H283 H290 E312 Y316 R324 E326
Enzyme Commision number
3.4.13.9
: Xaa-Pro dipeptidase.
Gene Ontology
Molecular Function
GO:0008237
metallopeptidase activity
GO:0016805
dipeptidase activity
GO:0046872
metal ion binding
GO:0102009
proline dipeptidase activity
Biological Process
GO:0006508
proteolysis
Cellular Component
GO:0005737
cytoplasm
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1wy2
,
PDBe:1wy2
,
PDBj:1wy2
PDBsum
1wy2
PubMed
UniProt
O58885
|PEPQ_PYRHO Xaa-Pro dipeptidase (Gene Name=pepQ)
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