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1K1X

Crystal structure of 4-alpha-glucanotransferase from thermococcus litoralis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004134molecular_function4-alpha-glucanotransferase activity
A0005975biological_processcarbohydrate metabolic process
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0030246molecular_functioncarbohydrate binding
A0102500molecular_functionbeta-maltose 4-alpha-glucanotransferase activity
B0003824molecular_functioncatalytic activity
B0004134molecular_function4-alpha-glucanotransferase activity
B0005975biological_processcarbohydrate metabolic process
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0030246molecular_functioncarbohydrate binding
B0102500molecular_functionbeta-maltose 4-alpha-glucanotransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 1601
ChainResidue
AASP392
AASP394
AASP396
AARG398
AGLU400

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 1602
ChainResidue
BGLU400
BASP392
BASP394
BASP396
BARG398

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 1603
ChainResidue
AASN248
BGLU60
BHOH1668
BHOH1681
BHOH1759

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TRS B 1604
ChainResidue
BHIS11
BGLU123
BASP214
BTRP357
BHOH1648
BHOH1663
BHOH1745
BHOH1808

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AGLU123
BGLU123

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
AASP214
BASP214

218853

PDB entries from 2024-04-24

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