Structure of PDB 5uw3 Chain A

Receptor sequence
>5uw3A (length=693) Species: 39387 (Gypsophila vaccaria) [Search protein sequence]
YPPVRRDETVVDDYFGVKVADPYRWLEDPNSEETKEFVDNQEKLANSVLE
ECELIDKFKQKIIDFVNFPRCGVPFRRANKYFHFYNSGLQAQNVFQMQDD
LDGKPEVLYDPNLREGGRSGLSLYSVSEDAKYFAFGIHSGLTEWVTIKIL
KTEDRSYLPDTLEWVKFSPAIWTHDNKGFFYCPYPPNQEARYHFLGTDQS
EDILLWRDLENPAHHLKCQITDDGKYFLLYILDGCDDANKVYCLDLTKLP
NGLESFAPFMKLIDSFDASYTAIANDGSVFTFQTNKDAPRKKLVRVDLNN
PSVWTDLVPESKKDLLESAHAVNENQLILRYLSDVKHVLEIRDLESGALQ
HRLPIDIGSVDGITARRRDSVVFFKFTSILTPGIVYQCDLKNDPTQLKIF
RESVVPDFDRSEFEVKQVFVPSKDGTKIPIFIAARKGISLDGSHPCEMHG
YGGFGINMMPTFSASRIVFLKHLGGVFCLANIRGGGEYGEEWHKAGFRDK
KQNVFDDFISAAEYLISSGYTKARRVAIEGGSNGGLLVAACINQRPDLFG
CAEANCGVMDMLRFHKFTLGYLWTGDYGCSDKEEEFKWLIKYSPIHNVRR
PWEQPGNEETQYPATMILTADHDDRVVPLHSFKLLATMQHVLCTSLEDSP
QKNPIIARIQRKAAHYGRATMTQIAEVADRYGFMAKALEAPWI
3D structure
PDB5uw3 Characterization of the macrocyclase involved in the biosynthesis of RiPP cyclic peptides in plants.
ChainA
Resolution1.96 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y481 S562 D653 H695
Catalytic site (residue number reindexed from 1) Y451 S532 D623 H665
Enzyme Commision number 3.4.21.-
3.4.21.26: prolyl oligopeptidase.
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 peptide A R81 F95 A102 N104 L132 F492 S493 A494 S495 T700 R70 F84 A91 N93 L121 F462 S463 A464 S465 T670
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
GO:0046872 metal ion binding
GO:0070012 oligopeptidase activity
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5uw3, PDBe:5uw3, PDBj:5uw3
PDBsum5uw3
PubMed28584123
UniProtR4P353

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