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5ZOL

Crystal structure of a three sites mutantion of FSAA complexed with HA and product

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 Residues4
Detailsbinding site for residue 4Y8 A 301
ChainResidue
AASP6
AASN28
ALYS85
ALW2302

site_idAC2
Number of Residues7
Detailsbinding site for residue LW2 A 302
ChainResidue
ASER166
A4Y8301
AASP6
AASN28
ATYR131
AASN133
AARG134

site_idAC3
Number of Residues2
Detailsbinding site for residue CL A 303
ChainResidue
ATHR7
ALEU188

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 A 304
ChainResidue
AALA62
ATHR63
ATHR64
AHOH445

site_idAC5
Number of Residues7
Detailsbinding site for residue LW2 B 302
ChainResidue
BASP6
BASN28
BTYR131
BARG134
BSER166
B4Y8301
BHOH407

site_idAC6
Number of Residues4
Detailsbinding site for residue SO4 B 303
ChainResidue
BALA62
BTHR63
BTHR64
BGLY67

site_idAC7
Number of Residues10
Detailsbinding site for residue LW2 C 302
ChainResidue
CASP6
CASN28
CTYR131
CASN133
CARG134
CSER166
CPHE167
CLYS168
C4Y8301
CHOH468

site_idAC8
Number of Residues1
Detailsbinding site for residue CL C 303
ChainResidue
CARG76

site_idAC9
Number of Residues7
Detailsbinding site for residue LW2 D 302
ChainResidue
DASP6
DASN28
DTYR131
DARG134
DSER166
DLYS168
D4Y8301

site_idAD1
Number of Residues4
Detailsbinding site for residue SO4 D 303
ChainResidue
DALA62
DTHR63
DTHR64
DGLY67

site_idAD2
Number of Residues6
Detailsbinding site for residue LW2 E 302
ChainResidue
EASP6
ETYR131
EASN133
EARG134
ESER166
ELYS168

site_idAD3
Number of Residues4
Detailsbinding site for residue SO4 E 303
ChainResidue
EARG217
ETHR218
ESER219
FGLN45

site_idAD4
Number of Residues6
Detailsbinding site for residue LW2 F 302
ChainResidue
FASP6
FTYR131
FARG134
FSER166
FLYS168
FHOH419

site_idAD5
Number of Residues2
Detailsbinding site for residue CL F 303
ChainResidue
FTHR7
FTHR31

site_idAD6
Number of Residues4
Detailsbinding site for residue SO4 F 304
ChainResidue
FALA62
FTHR63
FTHR64
FGLY67

site_idAD7
Number of Residues4
Detailsbinding site for residue LW1 G 302
ChainResidue
GASP6
GARG134
GSER166
GHOH487

site_idAD8
Number of Residues5
Detailsbinding site for residue SO4 G 303
ChainResidue
GALA62
GTHR63
GTHR64
GGLY67
GHOH463

site_idAD9
Number of Residues5
Detailsbinding site for residue LW2 H 302
ChainResidue
HASP6
HTYR131
HARG134
HSER166
HHOH470

site_idAE1
Number of Residues4
Detailsbinding site for residue SO4 H 303
ChainResidue
HALA62
HTHR63
HTHR64
HGLY67

site_idAE2
Number of Residues4
Detailsbinding site for residue LW2 I 302
ChainResidue
IASP6
IARG134
ISER166
ILYS168

site_idAE3
Number of Residues1
Detailsbinding site for residue CL I 303
ChainResidue
IARG76

site_idAE4
Number of Residues3
Detailsbinding site for residue SO4 I 304
ChainResidue
IALA62
ITHR63
ITHR64

site_idAE5
Number of Residues7
Detailsbinding site for residue LW2 J 302
ChainResidue
JASN28
JTYR131
JARG134
JSER166
JLYS168
JHOH436
JASP6

site_idAE6
Number of Residues4
Detailsbinding site for residue SO4 J 303
ChainResidue
JALA62
JTHR63
JTHR64
JGLY67

site_idAE7
Number of Residues13
Detailsbinding site for Di-peptide 4Y8 B 301 and LYS B 85
ChainResidue
BASP6
BTHR26
BTHR27
BASN28
BPHE57
BALA58
BTHR59
BVAL60
BVAL83
BVAL84
BVAL86
BLEU107
BLW2302

site_idAE8
Number of Residues13
Detailsbinding site for Di-peptide 4Y8 C 301 and LYS C 85
ChainResidue
CASP6
CTHR27
CASN28
CPHE57
CALA58
CTHR59
CVAL60
CVAL83
CVAL84
CVAL86
CLEU107
CTHR109
CLW2302

site_idAE9
Number of Residues11
Detailsbinding site for Di-peptide 4Y8 D 301 and LYS D 85
ChainResidue
DASP6
DTHR27
DASN28
DALA58
DTHR59
DVAL60
DVAL83
DVAL84
DVAL86
DLEU107
DLW2302

site_idAF1
Number of Residues13
Detailsbinding site for Di-peptide 4Y8 E 301 and LYS E 85
ChainResidue
EASP6
ETHR26
ETHR27
EASN28
EPHE57
EALA58
ETHR59
EVAL60
EVAL83
EVAL84
EVAL86
ELEU107
EHOH466

site_idAF2
Number of Residues13
Detailsbinding site for Di-peptide 4Y8 F 301 and LYS F 85
ChainResidue
FASP6
FTHR26
FTHR27
FASN28
FPHE57
FALA58
FTHR59
FVAL60
FVAL83
FVAL84
FVAL86
FLEU107
FHOH422

site_idAF3
Number of Residues12
Detailsbinding site for Di-peptide 4Y8 G 301 and LYS G 85
ChainResidue
GASP6
GTHR26
GTHR27
GASN28
GALA58
GTHR59
GVAL60
GVAL83
GVAL84
GVAL86
GLEU107
GHOH437

site_idAF4
Number of Residues13
Detailsbinding site for Di-peptide 4Y8 H 301 and LYS H 85
ChainResidue
HASP6
HTHR26
HTHR27
HASN28
HALA58
HTHR59
HVAL60
HVAL83
HVAL84
HVAL86
HLEU107
HTHR109
HHOH442

site_idAF5
Number of Residues12
Detailsbinding site for Di-peptide 4Y8 I 301 and LYS I 85
ChainResidue
IASP6
ITHR26
ITHR27
IASN28
IALA58
ITHR59
IVAL60
IVAL83
IVAL84
IVAL86
ILEU107
IHOH418

site_idAF6
Number of Residues12
Detailsbinding site for Di-peptide 4Y8 J 301 and LYS J 85
ChainResidue
JASP6
JTHR26
JTHR27
JASN28
JPHE57
JALA58
JTHR59
JVAL60
JVAL84
JVAL86
JLEU107
JTHR109

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

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

226707

PDB entries from 2024-10-30

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