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4RXG

Fructose-6-phosphate aldolase Q59E from E.coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0006000biological_processfructose metabolic process
A0016829molecular_functionlyase activity
A0016832molecular_functionaldehyde-lyase activity
A0042182biological_processketone catabolic process
A0042802molecular_functionidentical protein binding
A0097023molecular_functionfructose 6-phosphate aldolase activity
B0005737cellular_componentcytoplasm
B0005975biological_processcarbohydrate metabolic process
B0006000biological_processfructose metabolic process
B0016829molecular_functionlyase activity
B0016832molecular_functionaldehyde-lyase activity
B0042182biological_processketone catabolic process
B0042802molecular_functionidentical protein binding
B0097023molecular_functionfructose 6-phosphate aldolase activity
C0005737cellular_componentcytoplasm
C0005975biological_processcarbohydrate metabolic process
C0006000biological_processfructose metabolic process
C0016829molecular_functionlyase activity
C0016832molecular_functionaldehyde-lyase activity
C0042182biological_processketone catabolic process
C0042802molecular_functionidentical protein binding
C0097023molecular_functionfructose 6-phosphate aldolase activity
D0005737cellular_componentcytoplasm
D0005975biological_processcarbohydrate metabolic process
D0006000biological_processfructose metabolic process
D0016829molecular_functionlyase activity
D0016832molecular_functionaldehyde-lyase activity
D0042182biological_processketone catabolic process
D0042802molecular_functionidentical protein binding
D0097023molecular_functionfructose 6-phosphate aldolase activity
E0005737cellular_componentcytoplasm
E0005975biological_processcarbohydrate metabolic process
E0006000biological_processfructose metabolic process
E0016829molecular_functionlyase activity
E0016832molecular_functionaldehyde-lyase activity
E0042182biological_processketone catabolic process
E0042802molecular_functionidentical protein binding
E0097023molecular_functionfructose 6-phosphate aldolase activity
F0005737cellular_componentcytoplasm
F0005975biological_processcarbohydrate metabolic process
F0006000biological_processfructose metabolic process
F0016829molecular_functionlyase activity
F0016832molecular_functionaldehyde-lyase activity
F0042182biological_processketone catabolic process
F0042802molecular_functionidentical protein binding
F0097023molecular_functionfructose 6-phosphate aldolase activity
G0005737cellular_componentcytoplasm
G0005975biological_processcarbohydrate metabolic process
G0006000biological_processfructose metabolic process
G0016829molecular_functionlyase activity
G0016832molecular_functionaldehyde-lyase activity
G0042182biological_processketone catabolic process
G0042802molecular_functionidentical protein binding
G0097023molecular_functionfructose 6-phosphate aldolase activity
H0005737cellular_componentcytoplasm
H0005975biological_processcarbohydrate metabolic process
H0006000biological_processfructose metabolic process
H0016829molecular_functionlyase activity
H0016832molecular_functionaldehyde-lyase activity
H0042182biological_processketone catabolic process
H0042802molecular_functionidentical protein binding
H0097023molecular_functionfructose 6-phosphate aldolase activity
I0005737cellular_componentcytoplasm
I0005975biological_processcarbohydrate metabolic process
I0006000biological_processfructose metabolic process
I0016829molecular_functionlyase activity
I0016832molecular_functionaldehyde-lyase activity
I0042182biological_processketone catabolic process
I0042802molecular_functionidentical protein binding
I0097023molecular_functionfructose 6-phosphate aldolase activity
J0005737cellular_componentcytoplasm
J0005975biological_processcarbohydrate metabolic process
J0006000biological_processfructose metabolic process
J0016829molecular_functionlyase activity
J0016832molecular_functionaldehyde-lyase activity
J0042182biological_processketone catabolic process
J0042802molecular_functionidentical protein binding
J0097023molecular_functionfructose 6-phosphate aldolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 301
ChainResidue
AASP6
ATHR26
ATHR27
AASN28
ALYS85
ATYR131
AALA165
AGOL302

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 302
ChainResidue
AASN28
ASER166
AGOL301
AASP6

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 301
ChainResidue
BASP6
BTHR27
BASN28
BLYS85
BTYR131
BALA165
BGOL302

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 302
ChainResidue
BASP6
BASN28
BARG134
BSER166
BGOL301

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL C 301
ChainResidue
CASP6
CTHR26
CTHR27
CASN28
CLYS85
CTYR131
CALA165
CGOL302

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL C 302
ChainResidue
CASP6
CASN28
CARG134
CSER166
CGOL301
CHOH408

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL D 301
ChainResidue
DASP6
DTHR26
DTHR27
DASN28
DLYS85
DTYR131
DALA165
DGOL302

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL D 302
ChainResidue
DASP6
DASN28
DARG134
DSER166
DGOL301
DHOH446
DHOH494

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL E 301
ChainResidue
EASP6
ETHR27
EASN28
ELYS85
ETYR131
EALA165
EGOL302

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL E 302
ChainResidue
EASP6
EASN28
ETYR131
EARG134
ESER166
EGOL301
EHOH476

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL F 301
ChainResidue
FASP6
FTHR26
FTHR27
FASN28
FLYS85
FTYR131
FALA165
FGOL302

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL F 302
ChainResidue
FASP6
FASN28
FTYR131
FARG134
FSER166
FGOL301
FHOH509

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL G 301
ChainResidue
GASP6
GTHR27
GASN28
GLYS85
GTYR131
GALA165
GHOH469

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL H 301
ChainResidue
HASP6
HTHR27
HASN28
HLYS85
HTYR131
HALA165
HGOL302

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL H 302
ChainResidue
HARG134
HSER166
HGOL301
HASP6
HASN28
HTYR131

site_idBC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL I 301
ChainResidue
IASP6
ITHR27
IASN28
ILYS85
ITYR131
IALA165
IGOL302

site_idBC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL I 302
ChainResidue
IASP6
IASN28
IARG134
ISER166
IGOL301
IHOH464
IHOH475

site_idBC9
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 1PE I 303
ChainResidue
CGLY139
HARG171
HLEU174
HTYR197
IGLY113
IALA114
IALA115
IGLN116
ITHR145
IASP148
IHOH421

site_idCC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL J 301
ChainResidue
JASP6
JTHR26
JTHR27
JASN28
JLYS85
JTYR131
JALA165
JGOL302

site_idCC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL J 302
ChainResidue
JASP6
JASN28
JARG134
JSER166
JGOL301
JHOH426

site_idCC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL J 303
ChainResidue
JTHR7
JSER8
JASP9
JILE31
JALA34
JHOH430

Functional Information from PROSITE/UniProt
site_idPS00958
Number of Residues18
DetailsTRANSALDOLASE_2 Transaldolase active site. IvVKVPvTaEGLaAiKmL
ChainResidueDetails
AILE82-LEU99

site_idPS01054
Number of Residues9
DetailsTRANSALDOLASE_1 Transaldolase signature 1. GVTTNPSII
ChainResidueDetails
AGLY24-ILE32

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsACT_SITE: Schiff-base intermediate with substrate => ECO:0000269|PubMed:11120740, ECO:0000269|PubMed:12051943
ChainResidueDetails
ALYS85
JLYS85
BLYS85
CLYS85
DLYS85
ELYS85
FLYS85
GLYS85
HLYS85
ILYS85

224201

PDB entries from 2024-08-28

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