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2V9F

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
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A1275
ChainResidue
AASN29
AGLY31
AASN32
AHIS141
AHIS143
AHIS212
AZN1279

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A1276
ChainResidue
ASER270
AZN1281
AHOH2123
AHIS46
AHIS204

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A1277
ChainResidue
AALA131
AASP178
AGLN202
ALYS203
AHOH2124
AHOH2125

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A1278
ChainResidue
AASP39
AASN67
AASP157
AHOH2126

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1279
ChainResidue
AHIS141
AHIS143
AHIS212
AACT1275

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A1280
ChainResidue
AGLU27
AHIS143
AGLU171

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A1281
ChainResidue
AHIS46
AGLU200
AHIS204
AACT1276
AHOH2127

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:11976494, ECO:0000269|PubMed:12962479
ChainResidueDetails
AGLU117

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:11976494, ECO:0000269|PubMed:12962479
ChainResidueDetails
AHIS141
AHIS143
AHIS212

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

221051

PDB entries from 2024-06-12

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