Structure of PDB 8jmo Chain A Binding Site BS01

Receptor Information
>8jmo Chain A (length=258) Species: 2725 (unidentified prokaryotic organism) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SNPYQRGPNPTRSALTADGPFSVATYTVSRLSVSGFGGGVIYYPTGTSLT
FGGIAMSPGYTADASSLAWLGRRLASHGFVVLVINTNSRFDGPDSRASQL
SAALNYLRTSSPSAVRARLDANRLAVAGHAMGGGGTLRIAEQNPSLKAAV
PLTPWHTDKTFNTSVPVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYV
ELCNASHIAPNSNNAAISVYTISWMKLWVDNDTRYRQFLCNVNDPALCDF
RTNNRHCQ
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 chain8jmo Chain A Residue 401 [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]
PDB8jmo Remodeling the polymer-binding cavity to improve the efficacy of PBAT-degrading enzyme.
Resolution1.95 Å
Binding residue
(original residue number in PDB)		D193 T195
Binding residue
(residue number reindexed from 1)		D158 T160
Annotation score1
Enzymatic activity
Enzyme Commision number 3.1.1.101: poly(ethylene terephthalate) hydrolase.
3.1.1.74: cutinase.
Gene Ontology
Molecular Function
GO:0008126 acetylesterase activity
GO:0016787 hydrolase activity
GO:0050525 cutinase activity
GO:0052689 carboxylic ester hydrolase activity
Cellular Component
GO:0005576 extracellular region

View graph for
Molecular Function
View graph for
Cellular Component
External links
PDB RCSB:8jmo, PDBe:8jmo, PDBj:8jmo
PDBsum8jmo
PubMed37979420
UniProtG9BY57|PETH_UNKP Leaf-branch compost cutinase

[Back to BioLiP]