Structure of PDB 3emq Chain A

Receptor sequence
>3emqA (length=331) [Search protein sequence]
STEIPSLSASYANSFKIGAAVHTRMLQTEGEFIAKHYNSVTAENQMKFEE
VHPREHEYTFEAADEIVDFAVARGIGVRGHTLVWHNQTPAWMFEDASGGT
ASREMMLSRLKQHIDTVVGRYKDQIYAWDVVNEAIEDKTDLIMRDTKWLR
LLGEDYLVQAFNMAHEADPNALLFYNDYNETDPVKREKIYNLVRSLLDQG
APVHGIGMQGHWNIHGPSMDEIRQAIERYASLDVQLHVTELDLSVFRHED
QRTDLTEPTAEMAELQQKRYEDIFGLFREYRSNITSVTFWGVADNYTWLD
NFPVRGRKNWPFVFDTELQPKDSFWRIIGQD
3D structure
PDB3emq Structural insights into the specificity of Xyn10B from Paenibacillus barcinonensis and its improved stability by forced protein evolution.
ChainA
Resolution2.73 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 3.2.1.8: endo-1,4-beta-xylanase.
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 HAH A K48 H81 E134 Y179 Q210 E241 W291 W299 K47 H80 E133 Y178 Q209 E240 W290 W298
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0031176 endo-1,4-beta-xylanase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0045493 xylan catabolic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3emq, PDBe:3emq, PDBj:3emq
PDBsum3emq
PubMed19940147
UniProtO69231|XYNB_PAEBA Endo-1,4-beta-xylanase B (Gene Name=xynB)

[Back to BioLiP]