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Structure of PDB 5ofl Chain A

Receptor sequence
>5oflA (length=339) Species: 521460 (Caldicellulosiruptor bescii DSM 6725) [Search protein sequence]
DKMPDWNIPSLYESYKNDFRIGVAIPAKCLSNDTDRRMVLKHFNSITAEN
EMKPESLLAGQTSTGLNYRFSTADTFVDFANTNNIGIRGHTLVWHSQTPD
WFFKDSSGQRLTKDALLARLKQYIYDVVGRYKGKVYAWDVVNQAIDENQS
DGYRRSTWYEICGPEYIEKAFIWAHEADPNAKLFYNDYNTEISKKRDFIY
NMVKNLKSKGIPIHGIGMQCHINVNWPSVSEIENSIKLFSSIPGIEIHIT
QLDMSLYNYGSSENYSTPPQDLLQKQAQKYKELFTMLKKYTNVVKCVTFW
GLKDDYSWLRSFNGKNDWPLLLFEDYSAKPAYWAVIEAS
3D structure
PDB5ofl Insights into the roles of non-catalytic residues in the active site of a GH10 xylanase with activity on cellulose.
ChainA
Resolution1.871 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q140 N183 H218 Q248 D250
Catalytic site (residue number reindexed from 1) Q143 N186 H221 Q251 D253
Enzyme Commision number ?
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 BGC A N186 N220 W223 Y256 N189 N223 W226 Y259
BS02 BGC A Q140 Y185 H218 Q143 Y188 H221
BS03 BGC A H87 W91 Q140 Q216 H218 Q248 W305 H90 W94 Q143 Q219 H221 Q251 W308
BS04 BGC A E46 N47 W297 W305 E49 N50 W300 W308
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links

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