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5VSJ

Sco GlgEI-V279S in complex with a pyrolidene-based ethyl-phosphonate compound

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004556molecular_functionalpha-amylase activity
A0005975biological_processcarbohydrate metabolic process
A0009313biological_processoligosaccharide catabolic process
A0016757molecular_functionglycosyltransferase activity
A0016758molecular_functionhexosyltransferase activity
A0030979biological_processalpha-glucan biosynthetic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004556molecular_functionalpha-amylase activity
B0005975biological_processcarbohydrate metabolic process
B0009313biological_processoligosaccharide catabolic process
B0016757molecular_functionglycosyltransferase activity
B0016758molecular_functionhexosyltransferase activity
B0030979biological_processalpha-glucan biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue 9HV A 701
ChainResidue
ALYS264
AARG392
AASP394
AASN395
AGLU423
AASP480
ALYS534
ATYR535
AASN268
ASER279
ATRP281
AGLN324
ALYS355
ATYR357
AASP359
AILE360

site_idAC2
Number of Residues5
Detailsbinding site for residue TRS B 701
ChainResidue
BTYR639
BTYR646
BVAL647
BARG648
BHIS657

site_idAC3
Number of Residues17
Detailsbinding site for residue 9HV B 702
ChainResidue
BLYS264
BASN268
BSER279
BTRP281
BGLN324
BLYS355
BTYR357
BASP359
BILE360
BARG392
BASP394
BASN395
BGLU423
BASP480
BLYS534
BTYR535
BHOH821

Functional Information from PROSITE/UniProt
site_idPS00430
Number of Residues50
DetailsTONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. mpathhssatsaerptvvgripvldvrpvvqrgrrpakavtg.........................................................................ESFEVSAT
ChainResidueDetails
AMET1-THR50

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:21914799
ChainResidueDetails
AASP394
BASP394

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:21914799
ChainResidueDetails
AGLU423
BGLU423

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000305|PubMed:21914799
ChainResidueDetails
ALYS264
BLYS534
AGLN324
AASP359
AASN395
ALYS534
BLYS264
BGLN324
BASP359
BASN395

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000305|PubMed:21914799
ChainResidueDetails
AASP480
BASP480

221716

PDB entries from 2024-06-26

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