Structure of PDB 4hxf Chain B Binding Site BS02

Receptor Information
>4hxf Chain B (length=613) Species: 70601 (Pyrococcus horikoshii OT3) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
IEWDEKTFTKFAYLSDPRTRKNLVAYVLTKANLESNKYENTIVIENLEDG
SRKFIEDASMPRISPDGKKIAFMRFEKKTAQIWVADLKTLSAKKVLEAKN
IRSIEWNQDSRRLLAVGFKRREDEDFIFEDDVPAWFDNMGFFDGEKTTFW
VIDTEGEEVIEQFEKPRFSSGIWHGDSIVVSVPHRDVIPRYFKYWDIYLW
KDGEEEKLFEKVSFYAIDSDGERILLYGKPEKKYVSEHDKIYIYDGEVKG
ILDDIDREVAQAKIRNGKVYFTLFEEGSVNLYLWDGEVREIAKGKHWIMG
FDADERLIYLKETATRPAELYLWDGEERQLTDYNGLIFKKLKTFEPRHFR
FKSIDLELDGWYIKPEIKEGEKAPVIVFVHGGPKGMYGYYFKYEMQLMAS
KGYYIVYVNPRGSNGYSEDFALRVLERTGLEDFQDILNGIEEFLRLEPQA
DRERIGITGISYGGYMTNWALTQSDLFKAGISENGISYWLTSYAFSDIGL
WFDKEVIGDNPLENENYRKLSPLFYAKNVKAPLLLIHSLEDYRCPLDQSL
MFYHVLKDLGKEVYIAIFKKGAHGHSIRGSPRHRMKRYKLFMEFFERKLK
KYEEGFDVEKILK
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain4hxf Chain B Residue 703 [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]
PDB4hxf A Self-compartmentalizing Hexamer Serine Protease from Pyrococcus Horikoshii: SUBSTRATE SELECTION ACHIEVED THROUGH MULTIMERIZATION.
Resolution1.601 Å
Binding residue
(original residue number in PDB)		D244 E263
Binding residue
(residue number reindexed from 1)		D239 E258
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) H385 S466 Y467 D546 H580
Catalytic site (residue number reindexed from 1) H380 S461 Y462 D541 H575
Enzyme Commision number 3.4.19.1: acylaminoacyl-peptidase.
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008233 peptidase activity
GO:0008236 serine-type peptidase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4hxf, PDBe:4hxf, PDBj:4hxf
PDBsum4hxf
PubMed23632025
UniProtO58323

[Back to BioLiP]