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2VWT

Crystal structure of YfaU, a metal ion dependent class II aldolase from Escherichia coli K12 - Mg-pyruvate product complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0016151molecular_functionnickel cation binding
A0016829molecular_functionlyase activity
A0016832molecular_functionaldehyde-lyase activity
A0034214biological_processprotein hexamerization
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0106099molecular_function2-keto-3-deoxy-L-rhamnonate aldolase activity
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0016151molecular_functionnickel cation binding
B0016829molecular_functionlyase activity
B0016832molecular_functionaldehyde-lyase activity
B0034214biological_processprotein hexamerization
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0106099molecular_function2-keto-3-deoxy-L-rhamnonate aldolase activity
C0000287molecular_functionmagnesium ion binding
C0003824molecular_functioncatalytic activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0016151molecular_functionnickel cation binding
C0016829molecular_functionlyase activity
C0016832molecular_functionaldehyde-lyase activity
C0034214biological_processprotein hexamerization
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
C0106099molecular_function2-keto-3-deoxy-L-rhamnonate aldolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 301
ChainResidue
AGLN151
AGLU153
AASP179
APYR302
AHOH2040
AHOH2154

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PYR A 302
ChainResidue
APHE174
AGLY176
APRO177
AALA178
AASP179
ALEU216
AMG301
AARG74
AGLN151
AGLU153

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 301
ChainResidue
BGLN151
BGLU153
BASP179
BPYR302
BHOH2035
CHOH2094

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PYR B 302
ChainResidue
BARG74
BGLN151
BGLU153
BPHE174
BGLY176
BPRO177
BALA178
BASP179
BMG301
CHOH2094

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG C 301
ChainResidue
AHOH2112
CGLN151
CGLU153
CASP179
CPYR302
CHOH2112

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PYR C 302
ChainResidue
CARG74
CGLN151
CGLU153
CGLY176
CPRO177
CALA178
CASP179
CLEU216
CMG301

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A1257
ChainResidue
ATHR27
AALA29
AASP56
AHIS59
AHOH2201
AHOH2202
AHOH2203

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B1257
ChainResidue
BTHR27
BALA29
BASP56
BHIS59
BHOH2178
BHOH2179

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 C1257
ChainResidue
CTHR27
CTHR28
CALA29
CASP56
CHIS59
CHOH2157
CHOH2158

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL C1258
ChainResidue
CGLY78
CPRO97
CMET98
CGLN104

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS49
BHIS49
CHIS49

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING:
ChainResidueDetails
AGLN151
AALA178
AASP179
BGLN151
BALA178
BASP179
CGLN151
CALA178
CASP179

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:18754683
ChainResidueDetails
AGLU153
BGLU153
CGLU153

site_idSWS_FT_FI4
Number of Residues3
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AARG74
BARG74
CARG74

site_idSWS_FT_FI5
Number of Residues3
DetailsSITE: Increases basicity of active site His
ChainResidueDetails
AASP88
BASP88
CASP88

218853

PDB entries from 2024-04-24

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