Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1H54

Maltose phosphorylase from Lactobacillus brevis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016757molecular_functionglycosyltransferase activity
A0030246molecular_functioncarbohydrate binding
B0003824molecular_functioncatalytic activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0016757molecular_functionglycosyltransferase activity
B0030246molecular_functioncarbohydrate binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 1754
ChainResidue
ATYR488
AGLU489
AILE585
ALEU586
ASER588
ATYR590

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 B 1755
ChainResidue
BHIS671
BHOH2516
BHOH2865
BHOH2866
BHOH2867
BHOH2868
BHOH2869
BTYR352
BSER627
BSER628

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K B 1756
ChainResidue
BTYR488
BGLU489
BILE585
BLEU586
BSER588
BTYR590

Catalytic Information from CSA
site_idCSA1
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 11587643
ChainResidueDetails
AGLU487

site_idCSA2
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 11587643
ChainResidueDetails
BGLU487

site_idMCSA1
Number of Residues1
DetailsM-CSA 649
ChainResidueDetails
AGLU487proton donor

site_idMCSA2
Number of Residues1
DetailsM-CSA 649
ChainResidueDetails
BGLU487proton donor

238895

PDB entries from 2025-07-16

PDB statisticsPDBj update infoContact PDBjnumon