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2V9E

L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A- K248W-A273S)

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 Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1275
ChainResidue
AHIS141
AHIS143
AHIS212
AACT1281

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1276
ChainResidue
AHIS46
AHIS50
AACT1278
BHIS103

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN A1277
ChainResidue
AHIS204
AGLU200

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B1275
ChainResidue
BHIS141
BHIS143
BHIS212
BACT1278

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B1276
ChainResidue
AHIS103
AACT1279
AACT1280
BHIS50
BGLN52

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN B1277
ChainResidue
BGLU200
BHIS204

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A1278
ChainResidue
AHIS46
APHE49
AHIS50
AZN1276
AHOH2279
AHOH2280
BHIS103

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A1279
ChainResidue
ATYR55
AHIS103
AACT1280
AHOH2281
AHOH2282
BHIS50
BZN1276

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A1280
ChainResidue
APRO53
ATYR55
AHIS103
AACT1279
BHIS50
BZN1276

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A1281
ChainResidue
AASN29
AASN32
AHIS141
AHIS143
AGLU171
AHIS212
AZN1275

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT B1278
ChainResidue
BASN29
BASN32
BHIS141
BHIS143
BGLU171
BHIS212
BZN1275

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_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

221051

PDB entries from 2024-06-12

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