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3BQB

Hexagonal kristal form of 2-keto-3-deoxyarabinonate dehydratase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
A0019571biological_processD-arabinose catabolic process
A0044281biological_processsmall molecule metabolic process
A0046872molecular_functionmetal ion binding
A0051289biological_processprotein homotetramerization
X0000287molecular_functionmagnesium ion binding
X0003824molecular_functioncatalytic activity
X0016829molecular_functionlyase activity
X0016836molecular_functionhydro-lyase activity
X0019571biological_processD-arabinose catabolic process
X0044281biological_processsmall molecule metabolic process
X0046872molecular_functionmetal ion binding
X0051289biological_processprotein homotetramerization
Y0000287molecular_functionmagnesium ion binding
Y0003824molecular_functioncatalytic activity
Y0016829molecular_functionlyase activity
Y0016836molecular_functionhydro-lyase activity
Y0019571biological_processD-arabinose catabolic process
Y0044281biological_processsmall molecule metabolic process
Y0046872molecular_functionmetal ion binding
Y0051289biological_processprotein homotetramerization
Z0000287molecular_functionmagnesium ion binding
Z0003824molecular_functioncatalytic activity
Z0016829molecular_functionlyase activity
Z0016836molecular_functionhydro-lyase activity
Z0019571biological_processD-arabinose catabolic process
Z0044281biological_processsmall molecule metabolic process
Z0046872molecular_functionmetal ion binding
Z0051289biological_processprotein homotetramerization
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG Y 294
ChainResidue
YGLU143
YGLU145
YASP164
YLYS182

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG Z 294
ChainResidue
ZGLU143
ZGLU145
ZASP164
ZLYS182

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG X 294
ChainResidue
XGLU145
XASP164
XLYS182
XGLU143

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 294
ChainResidue
AGLU143
AGLU145
AASP164
ALYS182

Functional Information from PROSITE/UniProt
site_idPS00307
Number of Residues7
DetailsLECTIN_LEGUME_BETA Legume lectins beta-chain signature. LAVVLDS
ChainResidueDetails
ALEU146-SER152

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18448118","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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