Structure of PDB 5uw5 Chain C

Receptor sequence
>5uw5C (length=702) Species: 39387 (Gypsophila vaccaria) [Search protein sequence]
GFSKPLHYPPVRRDETVVDDYFGVKVADPYRWLEDPNSEETKEFVDNQEK
LANSVLEECELIDKFKQKIIDFVNFPRCGVPFRRANKYFHFYNSGLQAQN
VFQMQDDLDGKPEVLYDPNLREGGRSGLSLYSVSEDAKYFAFGIHSGLTE
WVTIKILKTEDRSYLPDTLEWVKFSPAIWTHDNKGFFYCPYPPVNQEARY
HFLGTDQSEDILLWRDLENPAHHLKCQITDDGKYFLLYILDGCDDANKVY
CLDLTKLPNGLESFRAPFMKLIDSFDASYTAIANDGSVFTFQTNKDAPRK
KLVRVDLNNPSVWTDLVPESKKDLLESAHAVNENQLILRYLSDVKHVLEI
RDLESGALQHRLPIDIGSVDGITARRRDSVVFFKFTSILTPGIVYQCDLK
NDPTQLKIFRESVVPDFDRSEFEVKQVFVPSKDGTKIPIFIAARKGISLD
GSHPCEMHGYGGFGINMMPTFSASRIVFLKHLGGVFCLANIRGGGEYGEE
WHKAGFRDKKQNVFDDFISAAEYLISSGYTKARRVAIEGGSNGGLLVAAC
INQRPDLFGCAEANCGVMDMLRFHKFTLGYLWTGDYGCSDKEEEFKWLIK
YSPIHNVRRPWEQPGNEETQYPATMILTADHDDRVVPLHSFKLLATMQHV
LCTSLEDSPQKNPIIARIQRKAAAYGRATMTQIAEVADRYGFMAKALEAP
WI
3D structure
PDB5uw5 Characterization of the macrocyclase involved in the biosynthesis of RiPP cyclic peptides in plants.
ChainC
Resolution2.94 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 A695
Catalytic site (residue number reindexed from 1) Y460 S541 D632 A674
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 C R81 F95 N104 L132 F492 S493 A494 S495 T700 R77 F91 N100 L128 F471 S472 A473 S474 T679
BS02 CA C E61 E64 E57 E60
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:5uw5, PDBe:5uw5, PDBj:5uw5
PDBsum5uw5
PubMed28584123
UniProtR4P353

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