Structure of PDB 2vqu Chain B

Receptor sequence
>2vquB (length=840) Species: 818 (Bacteroides thetaiotaomicron) [Search protein sequence]
NDTSEVMLLDTGWEFSQSGTEKWMPATVPGTVHQDLISHELLPNPFYGMN
EKKIQWVENEDWEYRTSFIVSEEQLNRDGIQLIFEGLDTYADVYLNGSLL
LKADNMFVGYTLPVKSVLRKGENHLYIYFHSPIRQTLPQYASNGFNYPAD
NDHHEKHLSVFSRKAPYSYGWDWGIRMVTSGVWRPVTLRFYDIATISDYY
VRQLSLTDENARLSNELIVNQIVPQKIPAEVRVNVSLNGTTVTEVKQQVT
LQPGINHITLPAEVTNPVRWMPNGWGTPTLYDFSAQIACGDRIVAEQSHR
IGLRTIRVVNEKDKDGESFYFEVNGIPMFAKGANYIPQDALLPNVTTERY
QTLFRDMKEANMNMVRIWGGGTYENNLFYDLADENGILVWQDFMFACTPY
PSDPTFLKRVEAEAVYNIRRLRNHASLAMWCGNNEILEALKYWGFEKKFT
PEVYQGLMHGYDKLFRELLPSTVKEFDSDRFYVHSSPYLANWGRPESWGT
GDSHNWGVWYGKKPFESLDTDLPRFMSEFGFQSFPEMKTIAAFAAPEDYQ
IESEVMNAHQKSSIGNSLIRTYMERDYIIPESFEDFVYVGLVLQGQGMRH
GLEAHRRNRPYCMGTLYAQLNDSWPVVSWSSIDYYGNWKALHYQAKRAFA
PVLINPIQQNDSLSVYLISDRLDTMEQMTLEMKVVDFDGKTLGKKIQVHS
LEVPANTSKCVYRAKLDGWLTPEDCRRSFLKLILKDKSGHQVAESVHFFR
KTKDLQLPPTSVSYQMKQTDGKCELTLFSSMLAKDIFIETPLQGARYSDN
FFDLLPGERKKVIITSPRIKKGEELPVNIKHIRETYKEHH
3D structure
PDB2vqu Structural and Biochemical Evidence for a Boat-Like Transition State in Beta-Mannosidases.
ChainB
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.25: beta-mannosidase.
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 NOY B D199 W200 W395 N461 E462 W533 Y537 E555 W656 D172 W173 W368 N434 E435 W506 Y510 E528 W629 MOAD: Ki=975nM
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004567 beta-mannosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006516 glycoprotein catabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2vqu, PDBe:2vqu, PDBj:2vqu
PDBsum2vqu
PubMed18408714
UniProtQ8AAK6

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