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3N9R

Class II fructose-1,6-bisphosphate aldolase from helicobacter pylori in complex with N-(4-hydroxybutyl)-phosphoglycolohydroxamic acid, a competitive inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004332molecular_functionfructose-bisphosphate aldolase activity
A0005975biological_processcarbohydrate metabolic process
A0006096biological_processglycolytic process
A0008270molecular_functionzinc ion binding
A0016832molecular_functionaldehyde-lyase activity
A0030388biological_processfructose 1,6-bisphosphate metabolic process
B0004332molecular_functionfructose-bisphosphate aldolase activity
B0005975biological_processcarbohydrate metabolic process
B0006096biological_processglycolytic process
B0008270molecular_functionzinc ion binding
B0016832molecular_functionaldehyde-lyase activity
B0030388biological_processfructose 1,6-bisphosphate metabolic process
e0004332molecular_functionfructose-bisphosphate aldolase activity
e0005975biological_processcarbohydrate metabolic process
e0006096biological_processglycolytic process
e0008270molecular_functionzinc ion binding
e0016832molecular_functionaldehyde-lyase activity
e0030388biological_processfructose 1,6-bisphosphate metabolic process
j0004332molecular_functionfructose-bisphosphate aldolase activity
j0005975biological_processcarbohydrate metabolic process
j0006096biological_processglycolytic process
j0008270molecular_functionzinc ion binding
j0016832molecular_functionaldehyde-lyase activity
j0030388biological_processfructose 1,6-bisphosphate metabolic process
K0004332molecular_functionfructose-bisphosphate aldolase activity
K0005975biological_processcarbohydrate metabolic process
K0006096biological_processglycolytic process
K0008270molecular_functionzinc ion binding
K0016832molecular_functionaldehyde-lyase activity
K0030388biological_processfructose 1,6-bisphosphate metabolic process
P0004332molecular_functionfructose-bisphosphate aldolase activity
P0005975biological_processcarbohydrate metabolic process
P0006096biological_processglycolytic process
P0008270molecular_functionzinc ion binding
P0016832molecular_functionaldehyde-lyase activity
P0030388biological_processfructose 1,6-bisphosphate metabolic process
U0004332molecular_functionfructose-bisphosphate aldolase activity
U0005975biological_processcarbohydrate metabolic process
U0006096biological_processglycolytic process
U0008270molecular_functionzinc ion binding
U0016832molecular_functionaldehyde-lyase activity
U0030388biological_processfructose 1,6-bisphosphate metabolic process
Z0004332molecular_functionfructose-bisphosphate aldolase activity
Z0005975biological_processcarbohydrate metabolic process
Z0006096biological_processglycolytic process
Z0008270molecular_functionzinc ion binding
Z0016832molecular_functionaldehyde-lyase activity
Z0030388biological_processfructose 1,6-bisphosphate metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 308
ChainResidue
AHIS83
AHIS180
AHIS210
ATD3311

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NA A 309
ChainResidue
AHIS210
ALYS251
AASN253
AGLN47
AHIS80
AASP82
AMET102
AGLU132

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CL A 310
ChainResidue
AASP104
ASER106
AGLU134
AHOH328
AHOH657
AHOH932
AHOH1126

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE TD3 A 311
ChainResidue
AHIS83
AHIS180
AGLY181
ALYS184
AHIS210
AGLY211
AALA212
ASER213
AASN253
AASP255
ATHR256
AZN308
AHOH374
AHOH807
AHOH2493

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 308
ChainResidue
BHIS83
BHIS180
BHIS210
BTD3311

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NA B 309
ChainResidue
BGLN47
BHIS80
BASP82
BMET102
BGLU132
BHIS210
BLYS251
BASN253

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CL B 310
ChainResidue
BASP104
BSER106
BGLU134
BHOH336
BHOH814
BHOH971
BHOH1010

site_idAC8
Number of Residues15
DetailsBINDING SITE FOR RESIDUE TD3 B 311
ChainResidue
BHIS83
BHIS180
BGLY181
BLYS184
BHIS210
BGLY211
BALA212
BSER213
BASN253
BASP255
BTHR256
BZN308
BHOH641
BHOH779
BHOH1770

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN K 308
ChainResidue
KHIS83
KHIS180
KHIS210
KTD3311

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NA K 309
ChainResidue
KGLN47
KHIS80
KASP82
KMET102
KGLU132
KHIS210
KLYS251
KASN253

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CL K 310
ChainResidue
KASP104
KSER106
KGLU134
KHOH330
KHOH589
KHOH1424
KHOH1565

site_idBC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE TD3 K 311
ChainResidue
KHOH2453
KHIS83
KHIS180
KGLY181
KLYS184
KHIS210
KGLY211
KALA212
KSER213
KASN253
KASP255
KTHR256
KZN308

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN P 308
ChainResidue
PHIS83
PHIS180
PHIS210
PTD3311

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NA P 309
ChainResidue
PGLN47
PHIS80
PASP82
PMET102
PGLU132
PHIS210
PLYS251
PASN253

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CL P 310
ChainResidue
PASP104
PSER106
PGLU134
PHOH339
PHOH397
PHOH1789
PHOH2376

site_idBC7
Number of Residues15
DetailsBINDING SITE FOR RESIDUE TD3 P 311
ChainResidue
AHOH2012
PASP82
PHIS83
PHIS180
PGLY181
PLYS184
PHIS210
PGLY211
PALA212
PSER213
PASN253
PASP255
PTHR256
PZN308
PHOH435

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN U 308
ChainResidue
UHIS83
UHIS180
UHIS210
UTD3311

site_idBC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NA U 309
ChainResidue
UGLN47
UHIS80
UASP82
UMET102
UGLU132
UHIS210
ULYS251
UASN253

site_idCC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL U 310
ChainResidue
UASP104
USER106
UGLU134
UHOH355
UHOH826

site_idCC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE TD3 U 311
ChainResidue
UASN23
UASP82
UHIS83
UHIS180
UGLY181
ULYS184
UHIS210
UGLY211
UALA212
USER213
UASN253
UASP255
UTHR256
UZN308

site_idCC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN Z 308
ChainResidue
ZHIS83
ZHIS180
ZHIS210
ZTD3311

site_idCC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NA Z 309
ChainResidue
ZGLN47
ZHIS80
ZASP82
ZMET102
ZGLU132
ZHIS210
ZLYS251
ZASN253

site_idCC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL Z 310
ChainResidue
ZASP104
ZSER106
ZGLU134
ZHOH324
ZHOH1520
ZHOH1875

site_idCC6
Number of Residues15
DetailsBINDING SITE FOR RESIDUE TD3 Z 311
ChainResidue
ZASP82
ZHIS83
ZHIS180
ZGLY181
ZLYS184
ZHIS210
ZGLY211
ZALA212
ZSER213
ZASN253
ZASP255
ZTHR256
ZZN308
ZHOH1876
ZHOH1983

site_idCC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN e 308
ChainResidue
eHIS83
eHIS180
eHIS210
eTD3311

site_idCC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA e 309
ChainResidue
eHIS80
eASP82
eMET102
eGLU132
eHIS210
eLYS251
eASN253

site_idCC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL e 310
ChainResidue
eASP104
eSER106
eGLU134
eHOH464

site_idDC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE TD3 e 311
ChainResidue
eASN23
eASP82
eHIS83
eHIS180
eGLY181
eLYS184
eHIS210
eGLY211
eALA212
eSER213
eASN253
eASP255
eTHR256
eZN308

site_idDC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN j 308
ChainResidue
jHIS83
jHIS180
jHIS210
jTD3311

site_idDC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NA j 309
ChainResidue
jGLN47
jHIS80
jASP82
jMET102
jGLU132
jHIS210
jLYS251
jASN253

site_idDC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL j 310
ChainResidue
jASP104
jSER106
jGLU134
jHOH943
jHOH1427

site_idDC5
Number of Residues15
DetailsBINDING SITE FOR RESIDUE TD3 j 311
ChainResidue
jASP82
jHIS83
jHIS180
jGLY181
jLYS184
jHIS210
jGLY211
jALA212
jSER213
jASN253
jASP255
jTHR256
jZN308
jHOH350
jHOH1682

Functional Information from PROSITE/UniProt
site_idPS00602
Number of Residues13
DetailsALDOLASE_CLASS_II_1 Fructose-bisphosphate aldolase class-II signature 1. Yph.IPVa.LHlDHG
ChainResidueDetails
ATYR72-GLY84

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

223532

PDB entries from 2024-08-07

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