Structure of PDB 3vig Chain A

Receptor sequence
>3vigA (length=472) Species: 60586 (Neotermes koshunensis) [Search protein sequence]
TVYTFPDEFKLGAATASYQIEGAWDENGKGPNIWDTLTHEHPDYVVDGAT
GDIADDSYHLYKEDVKILKELGAQVYRFSISWARVLPEGHDNIVNQDGID
YYNNLINELLANGIEPMVTMYHWDLPQALQDLGGWPNLVLAKYSENYARV
LFKNFGDRVKLWLTFNEPLTFMDGYASEIGMAPSINTPGIGDYLAAHTVI
HAHARIYHLYDQEFRAEQGGKVGISLNINWCEPATNSAEDRASCENYQQF
NLGLYAHPIFTEEGDYPAVLKDRVSRNSADEGYTDSRLPQFTAEEVEYIR
GTHDFLGINFYTALLGKSGVEGYEPSRYRDSGVILTQDAAWPISASSWLK
VVPWGFRKELNWIKNEYNNPPVFITENGFSDYGGLNDTGRVHYYTEHLKE
MLKAIHEDGVNVIGYTAWSLMDNFEWLRGYSEKFGIYAVDFEDPARPRIP
KESAKVLAEIMNTRKIPERFRD
3D structure
PDB3vig High-resolution structures of Neotermes koshunensis beta-glucosidase mutants provide insights into the catalytic mechanism and the synthesis of glucoconjugates
ChainA
Resolution0.99 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R103 H148 E193 T196 N335 Y337 E402
Catalytic site (residue number reindexed from 1) R77 H122 E167 T170 N309 Y311 E376
Enzyme Commision number 3.2.1.21: beta-glucosidase.
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 NOJ A Q45 H148 N192 E193 Y337 E402 W444 E451 F460 Q19 H122 N166 E167 Y311 E376 W418 E425 F434
BS02 EPE A E193 T196 N253 Y337 W374 R454 E167 T170 N227 Y311 W348 R428
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008422 beta-glucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3vig, PDBe:3vig, PDBj:3vig
PDBsum3vig
PubMed22751668
UniProtQ8T0W7

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