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3D5Y

High resolution crystal structure of 1,5-alpha-arabinanase catalytic mutant (AbnBE201A)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0016787molecular_functionhydrolase activity
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
AHOH1006
AHOH1018
AHOH1019
AHOH1052
AHOH1151

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"19505290","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"19505290","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19505290","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Important for catalytic activity, responsible for pKa modulation of the active site Glu and correct orientation of both the proton donor and substrate","evidences":[{"source":"PubMed","id":"19505290","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsSite: {"description":"Important for substrate recognition","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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