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2V9I

L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A- K248W-L274stop)

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
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005996biological_processmonosaccharide metabolic process
B0008994molecular_functionrhamnulose-1-phosphate aldolase activity
B0016829molecular_functionlyase activity
B0016830molecular_functioncarbon-carbon lyase activity
B0016832molecular_functionaldehyde-lyase activity
B0019299biological_processrhamnose metabolic process
B0019301biological_processrhamnose catabolic process
B0019323biological_processpentose catabolic process
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B1274
ChainResidue
BTRP21
BLYS23
BGLY24
BGLU27
BASP229
BHOH2030
BHOH2206

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A1274
ChainResidue
AGLY24
AGLU27
AASP229
AHOH2024
AHOH2204
ATRP21
ALYS23

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A1275
ChainResidue
AHIS141
AHIS143
AHIS212
AHOH2205
AHOH2206

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1276
ChainResidue
AGLU200
AHIS204
BHIS46
BASP47

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B1275
ChainResidue
BHIS141
BHIS143
BHIS212
BHOH2207

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1277
ChainResidue
AHIS46
AASP47
BGLU200
BHIS204

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
BGLU117

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:11976494, ECO:0000269|PubMed:12962479
ChainResidueDetails
AHIS141
AHIS143
AHIS212
BHIS141
BHIS143
BHIS212

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1gt7
ChainResidueDetails
AGLU117
AGLU171

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1gt7
ChainResidueDetails
BGLU117
BGLU171

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1gt7
ChainResidueDetails
AVAL174

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1gt7
ChainResidueDetails
BVAL174

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
BGLU117proton acceptor, proton donor
BHIS141metal ligand
BHIS143metal ligand
BGLU171proton donor
BHIS212metal ligand

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PDB entries from 2024-07-24

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