Structure of PDB 5uw5 Chain B Binding Site BS02

Receptor Information
>5uw5 Chain B (length=705) Species: 39387 (Gypsophila vaccaria) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ATSGFSKPLHYPPVRRDETVVDDYFGVKVADPYRWLEDPNSEETKEFVDN
QEKLANSVLEECELIDKFKQKIIDFVNFPRCGVPFRRANKYFHFYNSGLQ
AQNVFQMQDDLDGKPEVLYDPNLREGGRSGLSLYSVSEDAKYFAFGIHSG
LTEWVTIKILKTEDRSYLPDTLEWVKFSPAIWTHDNKGFFYCPYPPAVNQ
EARYHFLGTDQSEDILLWRDLENPAHHLKCQITDDGKYFLLYILDGCDDA
NKVYCLDLTKLPNGLESAPFMKLIDSFDASYTAIANDGSVFTFQTNKDAP
RKKLVRVDLNNPSVWTDLVPESKKDLLESAHAVNENQLILRYLSDVKHVL
EIRDLESGALQHRLPIDIGSVDGITARRRDSVVFFKFTSILTPGIVYQCD
LKNDPTQLKIFRESVVPDFDRSEFEVKQVFVPSKDGTKIPIFIAARKGIS
LDGSHPCEMHGYGGFGINMMPTFSASRIVFLKHLGGVFCLANIRGGGEYG
EEWHKAGFRDKKQNVFDDFISAAEYLISSGYTKARRVAIEGGSNGGLLVA
ACINQRPDLFGCAEANCGVMDMLRFHKFTLGYLWTGDYGCSDKEEEFKWL
IKYSPIHNVRRPWEQPGNEETQYPATMILTADHDDRVVPLHSFKLLATMQ
HVLCTSLEDSPQKNPIIARIQRKAAAYGRATMTQIAEVADRYGFMAKALE
APWID
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain5uw5 Chain B Residue 802 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB5uw5 Characterization of the macrocyclase involved in the biosynthesis of RiPP cyclic peptides in plants.
Resolution2.94 Å
Binding residue
(original residue number in PDB)		A717 E719
Binding residue
(residue number reindexed from 1)		A698 E700
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) A695
Catalytic site (residue number reindexed from 1) A676
Enzyme Commision number 3.4.21.-
3.4.21.26: prolyl oligopeptidase.
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5uw5, PDBe:5uw5, PDBj:5uw5
PDBsum5uw5
PubMed28584123
UniProtR4P353

[Back to BioLiP]