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4LQ1

Crystal Structure of E.Coli Branching Enzyme in complex with maltohexaose

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003844molecular_function1,4-alpha-glucan branching enzyme activity
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0005978biological_processglycogen biosynthetic process
A0043169molecular_functioncation binding
B0003824molecular_functioncatalytic activity
B0003844molecular_function1,4-alpha-glucan branching enzyme activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0005978biological_processglycogen biosynthetic process
B0043169molecular_functioncation binding
C0003824molecular_functioncatalytic activity
C0003844molecular_function1,4-alpha-glucan branching enzyme activity
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005975biological_processcarbohydrate metabolic process
C0005978biological_processglycogen biosynthetic process
C0043169molecular_functioncation binding
D0003824molecular_functioncatalytic activity
D0003844molecular_function1,4-alpha-glucan branching enzyme activity
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0005975biological_processcarbohydrate metabolic process
D0005978biological_processglycogen biosynthetic process
D0043169molecular_functioncation binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000250
ChainResidueDetails
AASP405
BASP405
CASP405
DASP405

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU458
BGLU458
CGLU458
DGLU458

227344

PDB entries from 2024-11-13

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