Structure of PDB 2xxl Chain B

Receptor sequence
>2xxlB (length=354) Species: 7227 (Drosophila melanogaster) [Search protein sequence]
DYADDCTTPDGDQGQCMPFSSCRTIEERLTEAQKAGQKVPADYASYLQKA
LCGEFNGVRHFCCPSANIQHNSKVMSLFKDENFDCGNFLSQRVSNGYEVK
LSSRPWMALLRYQQFGESRFLCGGAMISERYILTAAHCVHGLQNDLYEIR
LGEHRISTEEDCRQQGRKKKCAPPVVNVGIEKHLIHEKYDARHIMHDIAL
LKLNRSVPFQKHIKPICLPITDELKEKAEQISTYFVTGWGTTENGSSSDV
LLQANVPLQPRSACSQAYRRAVPLSQLCVGGGDLQDSCKGDSGGPLQAPA
QYLGEYAPKMVEFGIVSQGVVTCGQISLPGLYTNVGEYVQWITDTMASNG
LLES
3D structure
PDB2xxl Structure-Function Analysis of Grass Clip Serine Protease Involved in Drosophila Toll Pathway Activation.
ChainB
Resolution1.8 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) H163 D223 K315 G316 D317 S318 G319
Catalytic site (residue number reindexed from 1) H137 D197 K289 G290 D291 S292 G293
Enzyme Commision number 3.4.21.-
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 CA B E179 R181 T184 D187 E153 R155 T158 D161
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2xxl, PDBe:2xxl, PDBj:2xxl
PDBsum2xxl
PubMed21310954
UniProtQ9VB68|GRASS_DROME Serine protease grass (Gene Name=grass)

[Back to BioLiP]