Structure of PDB 5fmg Chain I

Receptor sequence
>5fmgI (length=186) Species: 5833 (Plasmodium falciparum) [Search protein sequence]
TTICGLVCQNAVILGADTRATEGPIVADKNCSKLHYISKNIWCAGAGVAG
DLEHTTLWLQHNVELHRLNTNTQPRVSMCVSRLTQELFKYVCAIVLGGVD
VNGPQLYGIHPHGSSCLLPFTALGSGSLNAMAVLEAKYRDNMTIEEGKNL
VCEAICAGIFNDLGSGGNVDICVITKDSYQHIRPYK
3D structure
PDB5fmg Structure and Function Based Design of Plasmodium-Selective Proteasome Inhibitors
ChainI
Resolution3.6 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) T1 D17 R19 K33 G47 S129 D166 S169
Catalytic site (residue number reindexed from 1) T1 D17 R19 K33 G47 S125 D162 S165
Enzyme Commision number 3.4.25.1: proteasome endopeptidase complex.
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 7F1 I T1 A20 T21 C31 S32 K33 G47 A49 L52 T1 A20 T21 C31 S32 K33 G47 A49 L52
Gene Ontology
Molecular Function
GO:0004298 threonine-type endopeptidase activity
Biological Process
GO:0051603 proteolysis involved in protein catabolic process
Cellular Component
GO:0005839 proteasome core complex

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:5fmg, PDBe:5fmg, PDBj:5fmg
PDBsum5fmg
PubMed26863983
UniProtQ8I6T3

[Back to BioLiP]