Structure of PDB 1wy2 Chain B

Receptor sequence
>1wy2B (length=347) Species: 70601 (Pyrococcus horikoshii OT3) [Search protein sequence]
NEKVKKIIEFMDKNSIDAVLIAKNPNVYYISGASPLAGGYILITGESATL
YVPELEYEMAKEESNIPVEKFKKMDEFYKALEGIKSLGIESSLPYGFIEE
LKKKANIKEFKKVDDVIRDMRIIKSEKEIKIIEKACEIADKAVMAAIEEI
TEGKKEREVAAKVEYLMKMNGAEKPAFDTIIASGYRSALPHGVASDKRIE
RGDLVVIDLGALYQHYNSDITRTIVVGSPNEKQKEIYEIVLEAQKKAVES
AKPGITAKELDSIARNIIAEYGYGEYFNHSLGHGVGLEVHEWPRVSQYDE
TVLREGMVITIEPGIYIPKIGGVRIEDTILITKNGSKRLTKTERELI
3D structure
PDB1wy2 Crystal Structure of the Prolidase from Pyrococcus horikoshii OT3
ChainB
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 B D212 D223 E330 D208 D219 E326
BS02 ZN B D223 H287 E316 E330 D219 H283 E312 E326
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
PDBsum1wy2
PubMed
UniProtO58885|PEPQ_PYRHO Xaa-Pro dipeptidase (Gene Name=pepQ)

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