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2UYU

L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT A88F- E192A)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005996biological_processmonosaccharide metabolic process
A0008994molecular_functionrhamnulose-1-phosphate aldolase activity
A0016829molecular_functionlyase activity
A0016830molecular_functioncarbon-carbon lyase activity
A0016832molecular_functionaldehyde-lyase activity
A0019299biological_processrhamnose metabolic process
A0019301biological_processrhamnose catabolic process
A0019323biological_processpentose catabolic process
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0005996biological_processmonosaccharide metabolic process
E0008994molecular_functionrhamnulose-1-phosphate aldolase activity
E0016829molecular_functionlyase activity
E0016830molecular_functioncarbon-carbon lyase activity
E0016832molecular_functionaldehyde-lyase activity
E0019299biological_processrhamnose metabolic process
E0019301biological_processrhamnose catabolic process
E0019323biological_processpentose catabolic process
E0042802molecular_functionidentical protein binding
E0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A1275
ChainResidue
AHIS141
AHIS143
AGLU171
AHIS212
AHOH2167

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE A1276
ChainResidue
EGLU254
EHOH2161
AHIS204
AHOH2123
AHOH2125
AHOH2126

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN E1275
ChainResidue
EHIS141
EHIS143
EGLU171
EHIS212
EHOH2174

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE E1276
ChainResidue
EHIS204
EHOH2122
EHOH2123
EHOH2124

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:11976494, ECO:0000269|PubMed:12962479
ChainResidueDetails
AGLU117
EGLU117

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:11976494, ECO:0000269|PubMed:12962479
ChainResidueDetails
AHIS141
AHIS143
AHIS212
EHIS141
EHIS143
EHIS212

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 645
ChainResidueDetails
AGLU117proton acceptor, proton donor
AHIS141metal ligand
AHIS143metal ligand
AGLU171proton donor
AHIS212metal ligand

site_idMCSA2
Number of Residues5
DetailsM-CSA 645
ChainResidueDetails
EGLU117proton acceptor, proton donor
EHIS141metal ligand
EHIS143metal ligand
EGLU171proton donor
EHIS212metal ligand

219869

PDB entries from 2024-05-15

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