Structure of PDB 2y24 Chain A

Receptor sequence
>2y24A (length=383) Species: 556 (Dickeya chrysanthemi) [Search protein sequence]
DTVKIDANVNYQIIQGFGGMSGVGWINDLTTEQINTAYGSGVGQIGLSIM
RVRIDPDSSKWNIQLPSARQAVSLGAKIMATPWSPPAYMKSNNSLINGGR
LLPANYSAYTSHLLDFSKYMQTNGAPLYAISIQNEPDWKPDYESCEWSGD
EFKSYLKSQGSKFGSLKVIVAESLGFNPALTDPVLKDSDASKYVSIIGGH
LYGTTPKPYPLAQNAGKQLWMTEHYVDSKQSANNWTSAIEVGTELNASMV
SNYSAYVWWYIRRSYGLLTEDGKVSKRGYVMSQYARFVRPGALRIQATEN
PQSNVHLTAYKNTDGKMVIVAVNTNDSDQMLSLNISNANVTKFEKYSTSA
SLNVEYGGSSQVDSSGKATVWLNPLSVTTFVSK
3D structure
PDB2y24 Structural Basis for Substrate Recognition by Erwinia Chrysanthemi Gh30 Glucuronoxylanase.
ChainA
Resolution1.39 Å
3D
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
Enzyme Commision number 3.2.1.136'
'3.2.1.8
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 XYP A W113 N164 E165 E253 W289 W83 N134 E135 E223 W259
BS02 GCV A Y255 W289 Y290 R293 Y295 Y225 W259 Y260 R263 Y265
Gene Ontology
Molecular Function
GO:0004348 glucosylceramidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0006665 sphingolipid metabolic process
GO:0045493 xylan catabolic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:2y24, PDBe:2y24, PDBj:2y24
PDBsum2y24
PubMed21501386
UniProtQ46961

[Back to BioLiP]