Structure of PDB 5oyd Chain A

Receptor sequence
>5oydA (length=370) Species: 498211 (Cellvibrio japonicus Ueda107) [Search protein sequence]
GLYPSYNTSPAAPDSTGMQSTAVQLAGKIRLGWNIGNTMEAIGGETAWGN
PMVSNELLKLVKDSGFDAVRIPVAWDQYANQESAEISAAWLNRVKQVVQM
AIDNELYVLINIHWDGGWLENNITPAKKDENNAKQKAFWEQIATHLRDFD
EHLLFAGTNEPNAENAEQMDVLNSYLQTFVDAVRSTGGKNAYRVLVLQGP
VTDIEKTNELWTHMPADTATDRLMAEVHFYTPYNFALMRQDESWGKQFYY
WGEGFLSTTDTERNPTWGEEATIDQLFDLMKTKFVDQGIPVVLGEFSAMR
RTNLTGDALTLHLAGRAYYHKYVTQQALARGLLPFYWDNGGNDNFSSGIF
NRQQNTVFDQQVLDALLEGA
3D structure
PDB5oyd In vitro and in vivo characterization of threeCellvibrio japonicusglycoside hydrolase family 5 members reveals potent xyloglucan backbone-cleaving functions.
ChainA
Resolution2.1 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.4: cellulase.
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 NBG A H208 N254 E255 H323 Y325 E390 W432 H113 N159 E160 H228 Y230 E295 W337 PDBbind-CN: -logKd/Ki=2.75,Kd=1.78mM
BS02 BGC A N132 W143 N434 N37 W48 N339 PDBbind-CN: -logKd/Ki=2.75,Kd=1.78mM
BS03 BGC A A142 W143 A47 W48 PDBbind-CN: -logKd/Ki=2.75,Kd=1.78mM
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0000272 polysaccharide catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5oyd, PDBe:5oyd, PDBj:5oyd
PDBsum5oyd
PubMed29467823
UniProtB3PD52

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