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3CU9

High resolution crystal structure of 1,5-alpha-L-arabinanase from Geobacillus Stearothermophilus

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031222biological_processarabinan catabolic process
A0046558molecular_functionarabinan endo-1,5-alpha-L-arabinosidase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 400
ChainResidue
AHIS271
AHOH1001
AHOH1011
AHOH1018
AHOH1022
AHOH1028
AHOH1258

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE GOL A 450
ChainResidue
ATRP84
APHE104
AILE146
AASP147
AGLU201
ACYS221
ATYR229
AHIS271
AHOH1003
AHOH1079
AHOH1083
AHOH1110
AHIS26
AASP27

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:19505290
ChainResidueDetails
AASP27

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:19505290
ChainResidueDetails
AGLU201

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:19505290
ChainResidueDetails
AASP27
AGLY105
AASN144
ASER164

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AHIS271

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Important for catalytic activity, responsible for pKa modulation of the active site Glu and correct orientation of both the proton donor and substrate => ECO:0000305|PubMed:19505290
ChainResidueDetails
AASP147

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Important for substrate recognition => ECO:0000250
ChainResidueDetails
AHIS271

219140

PDB entries from 2024-05-01

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