Structure of PDB 2fv0 Chain A

Receptor sequence
>2fv0A (length=377) Species: 84635 (Bacillus sp. GL1) [Search protein sequence]
MWQQAIGDALGITARNLKKFGDRFPHVSDGSNKYVLNDNTDWTDGFWSGI
LWLCYEYTGDEQYREGAVRTVASFRERLDRFENLDHHNIGFLYSLSAKAQ
WIVEKDESARKLALDAADVLMRRWRADAGIIQAWGPKGDPENGGRIIIDC
LLNLPLLLWAGEQTGDPEYRRVAEAHALKSRRFLVRGDDSSYHTFYFDPE
NGNAIRGGTHQGNTDGSTWTRGQAWGIYGFALNSRYLGNADLLETAKRMA
RHFLARVPEDGVVYWDFEVPQEPSSYRDSSASAITACGLLEIASQLDESD
PERQRFIDAAKTTVTALRDGYAERDDGEAEGFIRRGSYHVRGGISPDDYT
IWGDYYYLEALLRLERGVTGYWYERGR
3D structure
PDB2fv0 Substrate recognition by unsaturated glucuronyl hydrolase from Bacillus sp. GL1
ChainA
Resolution1.91 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.179: gellan tetrasaccharide unsaturated glucuronosyl hydrolase.
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 Y338 I344 S345 Y338 I344 S345
BS02 RAM A Y338 H339 Y338 H339
BS03 BGC A Q211 Y338 H339 Q211 Y338 H339
BS04 GAD A W42 H87 N88 F91 D149 R221 W42 H87 N88 F91 D149 R221
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0052757 chondroitin hydrolase activity
Biological Process
GO:0000272 polysaccharide catabolic process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:2fv0, PDBe:2fv0, PDBj:2fv0
PDBsum2fv0
PubMed16630576
UniProtQ9RC92|UGL_BACGL Unsaturated glucuronyl hydrolase (Gene Name=ugl)

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