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

3U95

Crystal structure of a putative alpha-glucosidase from Thermotoga neapolitana

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0046872molecular_functionmetal ion binding
C0003824molecular_functioncatalytic activity
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005975biological_processcarbohydrate metabolic process
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0016787molecular_functionhydrolase activity
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0046872molecular_functionmetal ion binding
D0003824molecular_functioncatalytic activity
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0005975biological_processcarbohydrate metabolic process
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0016787molecular_functionhydrolase activity
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0046872molecular_functionmetal ion binding
E0003824molecular_functioncatalytic activity
E0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
E0005975biological_processcarbohydrate metabolic process
E0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
E0016787molecular_functionhydrolase activity
E0016798molecular_functionhydrolase activity, acting on glycosyl bonds
E0046872molecular_functionmetal ion binding
F0003824molecular_functioncatalytic activity
F0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
F0005975biological_processcarbohydrate metabolic process
F0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
F0016787molecular_functionhydrolase activity
F0016798molecular_functionhydrolase activity, acting on glycosyl bonds
F0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN A 601
ChainResidue
ACYS181
AHIS210
AHOH1014

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN B 602
ChainResidue
BCYS181
BHIS210
BHOH1396

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN C 500
ChainResidue
CHOH1574
CHOH2182
CCYS181
CHIS210
CHOH1567

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN D 600
ChainResidue
DCYS181
DHIS210
DHOH1377

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN E 600
ChainResidue
ECYS181
EHIS210
EHOH1092
EHOH1575

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN F 600
ChainResidue
FCYS181
FHIS210
FASP267

249697

PDB entries from 2026-02-25

PDB statisticsPDBj update infoContact PDBjnumon