Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3VGB

Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0005992biological_processtrehalose biosynthetic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0033942molecular_function4-alpha-D-(1->4)-alpha-D-glucanotrehalose trehalohydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FLC A 1001
ChainResidue
AGLN323
AARG382
AGLY383
ALYS384
AASN448
AHOH2085
AHOH2104
AHOH2119

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1101
ChainResidue
AARG123
ALYS124
ATRP467
ASER537
AGLU548
AHOH2032
APRO114

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1102
ChainResidue
AGLU115
AGLY116
ASER163
APHE460
AHOH2050
AHOH2092

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1103
ChainResidue
ATYR152
AHIS192
ATRP215
AASP252
AGLU283
AASP377
AHOH2147

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:22334583
ChainResidueDetails
AASP252

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:22334583
ChainResidueDetails
AGLU283

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:22334583
ChainResidueDetails
AARG250
AASP308
AHIS376

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000305|PubMed:22334583
ChainResidueDetails
AASP377

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon