Structure of PDB 5uzw Chain C

Receptor sequence
>5uzwC (length=697) Species: 39387 (Gypsophila vaccaria) [Search protein sequence]
GFSKPLHYPPVRRDETVVDDYFGVKVADPYRWLEDPNSEETKEFVDNQEK
LANSVLEECELIDKFKQKIIDFVNFPRCGVPFRRANKYFHFYNSGLQAQN
VFQMQDDLDGKPEVLYDPNLREGGRSGLSLYSVSEDAKYFAFGIHSGLTE
WVTIKILKTEDRSYLPDTLEWVKFSPAIWTHDNKGFFYCPYPPVNQEARY
HFLGTDQSEDILLWRDLENPAHHLKCQITDDGKYFLLYILDGCDDANKVY
CLDLTKLPNGLESFRAPFMKLIDSFDASYTAIANDGSVFTFQTNKDAPRK
KLVRVDLNNPSVWTDLVPESKKDLLESAHAVNENQLILRYLSDVKHVLEI
RDLESGALQHRLPIDIGSVDGITARRRDSVVFFKFTSILTPGIVYQCDLK
NDPTQLKIFRESVVPDFDRSEFEVKQVFVPSKDGTKIPIFIAARKGISLD
GSHPCEMHGYGGFGINMMPTFSASRIVFLKHLGGVFCLANIRGGGEYGEE
WHKAGFRDKKQNVFDDFISAAEYLISSGYTKARRVAIEGGSNGGLLVAAC
INQRPDLFGCAEANCGVMDMLRFHKFTLGYLWTGDYGCSDKEEEFKWLIK
YSPIHNVRRPWEQPGNEETQYPATMILTADHDDRVVPLHSFKLLATMQHV
LCTSLEDSPQKNPIIARIQRGRATMTQIAEVADRYGFMAKALEAPWI
3D structure
PDB5uzw Characterization of the macrocyclase involved in the biosynthesis of RiPP cyclic peptides in plants.
ChainC
Resolution2.82 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
Catalytic site (residue number reindexed from 1) Y460 S541 D632
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 A102 N104 L132 F492 S493 A494 S495 T701 R77 F91 A98 N100 L128 F471 S472 A473 S474 T674
BS02 ZPR C H239 Y481 F484 S562 N563 W603 H223 Y460 F463 S541 N542 W582
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:5uzw, PDBe:5uzw, PDBj:5uzw
PDBsum5uzw
PubMed28584123
UniProtR4P353

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