Structure of PDB 3hhi Chain A

Receptor sequence
>3hhiA (length=258) Species: 5691 (Trypanosoma brucei) [Search protein sequence]
SILPKRRFTEEEARAPLPSSFDSAEAWPNCPTIPQIADQSACGSCWAVAA
ASAMSDRFCTMGGVQDVHISAGDLLACCSDCGDGCNGGDPDRAWAYFSST
GLVSDYCQPYPFPHCSHHSKSKNGYPPCSQFNFDTPKCDYTCDDPTIPVV
NYRSWTSYALQGEDDYMRELFFRGPFEVAFDVYEDFIAYNSGVYHHVSGQ
YLGGHAVRLVGWGTSNGVPYWKIANSWNTEWGMDGYFLIRRGSSECGIED
GGSAGIPL
3D structure
PDB3hhi Crystal Structures of TbCatB and rhodesain, potential chemotherapeutic targets and major cysteine proteases of Trypanosoma brucei
ChainA
Resolution1.6 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) Q116 C122 H282 N302
Catalytic site (residue number reindexed from 1) Q39 C45 H205 N225
Enzyme Commision number 3.4.22.-
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 074 A Q116 G120 C122 W123 G164 G165 H194 H195 G281 H282 W304 Q39 G43 C45 W46 G87 G88 H117 H118 G204 H205 W227
Gene Ontology
Molecular Function
GO:0004197 cysteine-type endopeptidase activity
GO:0008233 peptidase activity
GO:0008234 cysteine-type peptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0010608 post-transcriptional regulation of gene expression
GO:0051603 proteolysis involved in protein catabolic process
Cellular Component
GO:0005615 extracellular space
GO:0005764 lysosome

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:3hhi, PDBe:3hhi, PDBj:3hhi
PDBsum3hhi
PubMed20544024
UniProtQ6R7Z5

[Back to BioLiP]