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2V5K

Class II aldolase HpcH - magnesium - oxamate complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0010124biological_processphenylacetate catabolic process
A0016829molecular_functionlyase activity
A0016832molecular_functionaldehyde-lyase activity
A0043863molecular_function4-hydroxy-2-ketopimelate aldolase activity
A0046872molecular_functionmetal ion binding
A1901023biological_process4-hydroxyphenylacetate catabolic process
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0010124biological_processphenylacetate catabolic process
B0016829molecular_functionlyase activity
B0016832molecular_functionaldehyde-lyase activity
B0043863molecular_function4-hydroxy-2-ketopimelate aldolase activity
B0046872molecular_functionmetal ion binding
B1901023biological_process4-hydroxyphenylacetate catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 301
ChainResidue
AGLN147
AGLU149
AASP175
AOXM302
AHOH2027
AHOH2085

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE OXM A 302
ChainResidue
AGLY172
APRO173
AALA174
AASP175
ALEU212
AMG301
AHOH2085
AARG70
AGLN147
AGLU149

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 301
ChainResidue
BGLU149
BASP175
BOXM302
BHOH2031
BHOH2096

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE OXM B 302
ChainResidue
BARG70
BGLN147
BGLU149
BGLY172
BPRO173
BALA174
BASP175
BLEU212
BMG301
BHOH2096

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A1260
ChainResidue
ALYS6
ALYS10
AARG109
AGLU164
AGLY165
AASP167
AHOH2109

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B1260
ChainResidue
BLYS6
BLYS10
BARG109
BGLU164
BGLY165
BASP167

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17881002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18775708","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17881002","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17881002","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"17881002","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Increases basicity of active site His","evidences":[{"source":"PubMed","id":"17881002","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dxe
ChainResidueDetails
AHIS45
AARG70

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dxe
ChainResidueDetails
BHIS45
BARG70

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PDB entries from 2025-08-06

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