Structure of PDB 4qaw Chain F

Receptor sequence
>4qawF (length=531) Species: 198119 (Paenibacillus barcinonensis) [Search protein sequence]
ASDANINLSSEKQLIKGFGGINHPAWIGDLTAAQRETAFGNGQNQLGFSI
LRIYVDDNRNNWYREVATAKRAIEQGALVFASPWNPPSDMVETFNRNGAS
AKRLKYDKYAAYAQHLNDFVTFMKNNGVDLYAISVQNEPDYAHDWTWWTP
QEILRFMKENAGSIQGTRVMAPESFQYLKNISDPILNDPQALANMDILGA
HTYGTQIKDFAYPLFKQKGAGKELWMTEVYVPNSDNNSADRWPEALDVSY
HMHNAMVEGDFQAYVWWYIRRQYGPMKEDGTISKRGYNMAHFSKFVRPGY
VRVDATKNPDTNTYVSAYKGDNKVVIVAINRGTSAASQRFVLQNGNASTV
SSYVTDSSRNLASLAPINVSNGAFTAQLPAQSVTTFVANLSGGNSGGNTG
TTYEAETGTTLTDAVVETLYPGYTGSGYVNFNAYTNSAIEWNAINNMTTG
TKNVKFRYALESGTRNLDIYVNGTKVLSNEPFTETGSWSTWGEKTIQVAM
NSGVNTLRIVTTGTEGPNMDNITVTASAKGE
3D structure
PDB4qaw Structural Analysis of Glucuronoxylan-specific Xyn30D and Its Attached CBM35 Domain Gives Insights into the Role of Modularity in Specificity.
ChainF
Resolution2.4 Å
3D
structure
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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 CA F E407 E409 T427 G430 D523 E404 E406 T424 G427 D520
BS02 CA F N433 E518 N430 E515
Gene Ontology
Molecular Function
GO:0004348 glucosylceramidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0030246 carbohydrate binding
GO:0031176 endo-1,4-beta-xylanase activity
GO:0046872 metal ion binding
Biological Process
GO:0006665 sphingolipid metabolic process
GO:0045493 xylan catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4qaw, PDBe:4qaw, PDBj:4qaw
PDBsum4qaw
PubMed25202007
UniProtH6WCZ0

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