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3THI

THIAMINASE I FROM BACILLUS THIAMINOLYTICUS

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0009230biological_processthiamine catabolic process
A0016740molecular_functiontransferase activity
A0050332molecular_functionthiamine pyridinylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 380
ChainResidue
AHIS282
AHIS282
APRO283
APRO283
AGLU284
ALEU285

site_idNUC
Number of Residues1
DetailsCYS 113 IS THE ACTIVE SITE NUCLEOPHILE.
ChainResidue
ACYS113

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile
ChainResidueDetails
ACYS113

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AGLU241

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 357
ChainResidueDetails
ACYS113activator, covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
AGLU241activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AASP272electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, steric role

220472

PDB entries from 2024-05-29

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