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1KWG

Crystal structure of Thermus thermophilus A4 beta-galactosidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004565molecular_functionbeta-galactosidase activity
A0005975biological_processcarbohydrate metabolic process
A0006012biological_processgalactose metabolic process
A0009341cellular_componentbeta-galactosidase complex
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 801
ChainResidue
ATYR6
ATYR7
ATRP11
AARG351
AARG353

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 804
ChainResidue
AGLY535
AHOH875
AHOH927
AHOH1424

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACT A 805
ChainResidue
AARG560

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 806
ChainResidue
ACYS106
ACYS150
ACYS152
ACYS155

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MPD A 802
ChainResidue
APRO275

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MPD A 803
ChainResidue
AALA433
AARG436
APRO573
AGLY577
AHOH865
AHOH902
AHOH984

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
AGLU141

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AGLU312

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:12215416
ChainResidueDetails
AARG102
AASN140
ATRP320

site_idSWS_FT_FI4
Number of Residues5
DetailsBINDING:
ChainResidueDetails
ACYS106
ACYS150
ACYS152
ACYS155
AGLU360

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cz1
ChainResidueDetails
AGLU141
AASN241

219515

PDB entries from 2024-05-08

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