Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1GVF

Structure of tagatose-1,6-bisphosphate aldolase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0008270molecular_functionzinc ion binding
A0009025molecular_functiontagatose-bisphosphate aldolase activity
A0016829molecular_functionlyase activity
A0016832molecular_functionaldehyde-lyase activity
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0051289biological_processprotein homotetramerization
A1902494cellular_componentcatalytic complex
A2001059biological_processD-tagatose 6-phosphate catabolic process
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0008270molecular_functionzinc ion binding
B0009025molecular_functiontagatose-bisphosphate aldolase activity
B0016829molecular_functionlyase activity
B0016832molecular_functionaldehyde-lyase activity
B0032991cellular_componentprotein-containing complex
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0051289biological_processprotein homotetramerization
B1902494cellular_componentcatalytic complex
B2001059biological_processD-tagatose 6-phosphate catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 288
ChainResidue
AHIS83
AHIS180
AHIS208
APGH287

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 289
ChainResidue
APGH287
AALA179
AGLY181
ATYR183
AGLY209
ASER211

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 288
ChainResidue
BHIS83
BHIS180
BHIS208
BPGH287

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 289
ChainResidue
BALA179
BGLY181
BTYR183
BGLY209
BSER211
BPGH287

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PGH A 287
ChainResidue
AASP82
AHIS83
AALA179
AHIS180
AGLY181
AHIS208
AGLY209
AALA210
ASER211
AASN230
AVAL231
AALA232
ATHR233
AZN288
ANA289
AHOH2347
AHOH2348

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A1289
ChainResidue
ASER2
ASER70
AHOH2349
AHOH2350
BEDO1291

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A1290
ChainResidue
ALEU9
APRO44
AVAL45
APRO76
ALEU77
AALA78
AHOH2117

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A1291
ChainResidue
AASP190
AARG193
AGLU196

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A1292
ChainResidue
AGLN32
AGLU36
ATYR73

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A1293
ChainResidue
ATYR63
AHIS95
AALA96
AHOH2352

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A1294
ChainResidue
ALEU9
AASP12
ATYR18
APRO44
AARG283
AILE284
AHOH2353

site_idBC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PGH B 287
ChainResidue
BASN24
BASP82
BHIS83
BALA179
BHIS180
BGLY181
BHIS208
BGLY209
BALA210
BSER211
BASN230
BVAL231
BALA232
BTHR233
BZN288
BNA289
BHOH2296

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B1288
ChainResidue
BPRO44
BVAL45
BPRO76
BLEU77
BALA78
BHOH2298

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B1289
ChainResidue
BSER2
BSER70
BMET75
BHOH2299
BHOH2300
BHOH2301
BHOH2302

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B1290
ChainResidue
BHIS95
BALA96
BHOH2303

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B1291
ChainResidue
AASN74
APRO76
AEDO1289
BHIS95
BGLN127
BEDO1292

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B1292
ChainResidue
AASN74
BHIS95
BGLU199
BEDO1291

site_idBC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B1293
ChainResidue
BSER106
BPHE108
BARG137
BHOH2132

site_idCC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B1294
ChainResidue
BVAL114
BLYS115
BLYS118
BHOH2136
BHOH2140
BHOH2304

site_idCC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B1295
ChainResidue
BARG91
BASP122
BPHE123
BHOH2305

Functional Information from PROSITE/UniProt
site_idPS00602
Number of Residues14
DetailsALDOLASE_CLASS_II_1 Fructose-bisphosphate aldolase class-II signature 1. TtynMPLa.LHlDHH
ChainResidueDetails
ATHR71-HIS84

site_idPS00806
Number of Residues12
DetailsALDOLASE_CLASS_II_2 Fructose-bisphosphate aldolase class-II signature 2. VEaELGrlGGvE
ChainResidueDetails
AVAL131-GLU142

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:11940603
ChainResidueDetails
AASP82
BASP82

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:11940603
ChainResidueDetails
AHIS83
AHIS180
AHIS208
BHIS83
BHIS180
BHIS208

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AGLY181
AGLY209
AASN230
BGLY181
BGLY209
BASN230

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b57
ChainResidueDetails
AASP82
AASN230

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b57
ChainResidueDetails
BASP82
BGLU150
BASN230

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon