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4RZ4

Fructose-6-phosphate aldolase Q59E Y131F 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 Residues5
DetailsBINDING SITE FOR RESIDUE PGE A 301
ChainResidue
AASP6
AASN28
ALYS85
APHE131
APGE302

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGE A 302
ChainResidue
AHOH439
AARG134
ASER166
APGE301
AHOH430

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 303
ChainResidue
AARG134
ALYS168
AHOH495
BLYS206

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 304
ChainResidue
AHIS150
AVAL162
AGLU182

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGE B 301
ChainResidue
BASP6
BASN28
BLYS85
BPHE131
BPGE302

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PGE B 302
ChainResidue
BASN28
BARG134
BSER166
BPGE301
BHOH409
BHOH417
BHOH468

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 303
ChainResidue
BARG134
BLYS168
BHOH468
BHOH506
CLYS206

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 304
ChainResidue
BHIS150
BVAL162
BGLU182

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PGE C 301
ChainResidue
CASP6
CASN28
CLYS85
CPGE302

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PGE C 302
ChainResidue
CASN28
CARG134
CSER166
CPGE301
CHOH426
CHOH430
CHOH452

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 C 303
ChainResidue
CARG134
CLYS168
CHOH452
CHOH461
CHOH506
DLYS206

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL C 304
ChainResidue
CHIS150
CVAL162
CGLU182

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGE D 301
ChainResidue
DASP6
DASN28
DLYS85
DPHE131
DPGE302

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PGE D 302
ChainResidue
DASN28
DARG134
DSER166
DPGE301
DHOH407
DHOH431

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 D 303
ChainResidue
DARG134
DLYS168
ELYS206

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL D 304
ChainResidue
DHIS150
DVAL162
DGLU182

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PGE E 301
ChainResidue
EASP6
EASN28
ELYS85
EPGE302

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PGE E 302
ChainResidue
EARG134
ESER166
EPGE301
EHOH423
EHOH425
EHOH444

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 E 303
ChainResidue
ALYS206
EARG134
ELYS168
EHOH444

site_idCC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL E 304
ChainResidue
EHIS150
EVAL162
EGLU182

site_idCC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGE F 301
ChainResidue
FASP6
FASN28
FLYS85
FPHE131
FPGE302

site_idCC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PGE F 302
ChainResidue
FHOH412
FHOH426
FHOH511
FARG134
FSER166
FPGE301

site_idCC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 F 303
ChainResidue
FARG134
FLYS168
FHOH484
FHOH511
JLYS206

site_idCC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL F 304
ChainResidue
FHIS150
FVAL162
FGLU182

site_idCC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PGE G 301
ChainResidue
GASP6
GASN28
GLYS85
GPGE302

site_idCC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PGE G 302
ChainResidue
GARG134
GSER166
GPGE301
GHOH426
GHOH429
GHOH468

site_idCC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 G 303
ChainResidue
FLYS206
GARG134
GLYS168
GHOH468
GHOH486
GHOH547

site_idDC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL G 304
ChainResidue
GHIS150
GVAL162
GGLU182

site_idDC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGE H 301
ChainResidue
HASP6
HASN28
HLYS85
HPHE131
HPGE302

site_idDC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PGE H 302
ChainResidue
HASN28
HARG134
HSER166
HPGE301
HHOH453
HHOH468
HHOH516

site_idDC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 H 303
ChainResidue
GLYS206
HARG134
HLYS168
HHOH516

site_idDC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL H 304
ChainResidue
HHIS150
HVAL162
HGLU182

site_idDC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGE I 301
ChainResidue
IASP6
IASN28
ILYS85
IPHE131
IPGE302

site_idDC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGE I 302
ChainResidue
IARG134
ISER166
IPGE301
IHOH424
IHOH463

site_idDC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 I 303
ChainResidue
HLYS206
IARG134
ILYS168
IHOH490

site_idDC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL I 304
ChainResidue
IHIS150
IVAL162
IGLU182

site_idEC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGE J 301
ChainResidue
JASP6
JASN28
JLYS85
JPHE131
JPGE302

site_idEC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PGE J 302
ChainResidue
JARG134
JSER166
JPGE301
JHOH419
JHOH449
JHOH526

site_idEC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 J 303
ChainResidue
JARG134
JLYS168
JHOH502
JHOH526
JHOH548

site_idEC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL J 304
ChainResidue
JHIS150
JVAL162
JGLU182

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
BLYS85
CLYS85
DLYS85
ELYS85
FLYS85
GLYS85
HLYS85
ILYS85
JLYS85

219869

PDB entries from 2024-05-15

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