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4HA3

Structure of beta-glycosidase from Acidilobus saccharovorans in complex with Tris

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004565molecular_functionbeta-galactosidase activity
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE TRS A 501
ChainResidue
AGLN19
ATRP431
AGOL506
AHOH1007
AHOH1113
AHOH1114
AHIS152
ATRP153
AASN207
AGLU208
ATYR320
AGLU385
ATRP423
AGLU430

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 502
ChainResidue
AGLU391
AARG438
AMET443
AARG454
APRO481
AHOH744
AHOH820

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 503
ChainResidue
AVAL112
AGLU114
AHOH730
AHOH880
AHOH887

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 504
ChainResidue
AGLY47
ASER50
AALA432
AHOH665
AHOH674
AHOH846

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 505
ChainResidue
AASP393
AASP393
AHOH613
AHOH613
AHOH652
AHOH652

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 506
ChainResidue
APHE224
APHE357
AGLU430
ATRS501
AHOH671
AHOH1116

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG A 507
ChainResidue
AARG322
AALA350
AHOH793
AHOH1058

Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. LLVTENGIA
ChainResidueDetails
ALEU381-ALA389

site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FlFGwSqAGFQsEmG
ChainResidueDetails
APHE9-GLY23

222415

PDB entries from 2024-07-10

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