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

3HNO

Crystal Structure of Pyrophosphate-dependent phosphofructokinase from Nitrosospira multiformis. Northeast Structural Genomics Consortium target id NmR42

Functional Information from GO Data
ChainGOidnamespacecontents
A0003872molecular_function6-phosphofructokinase activity
A0005737cellular_componentcytoplasm
A0006002biological_processfructose 6-phosphate metabolic process
A0006096biological_processglycolytic process
A0016301molecular_functionkinase activity
A0046835biological_processcarbohydrate phosphorylation
A0046872molecular_functionmetal ion binding
A0047334molecular_functiondiphosphate-fructose-6-phosphate 1-phosphotransferase activity
A0061615biological_processglycolytic process through fructose-6-phosphate
B0003872molecular_function6-phosphofructokinase activity
B0005737cellular_componentcytoplasm
B0006002biological_processfructose 6-phosphate metabolic process
B0006096biological_processglycolytic process
B0016301molecular_functionkinase activity
B0046835biological_processcarbohydrate phosphorylation
B0046872molecular_functionmetal ion binding
B0047334molecular_functiondiphosphate-fructose-6-phosphate 1-phosphotransferase activity
B0061615biological_processglycolytic process through fructose-6-phosphate
C0003872molecular_function6-phosphofructokinase activity
C0005737cellular_componentcytoplasm
C0006002biological_processfructose 6-phosphate metabolic process
C0006096biological_processglycolytic process
C0016301molecular_functionkinase activity
C0046835biological_processcarbohydrate phosphorylation
C0046872molecular_functionmetal ion binding
C0047334molecular_functiondiphosphate-fructose-6-phosphate 1-phosphotransferase activity
C0061615biological_processglycolytic process through fructose-6-phosphate
D0003872molecular_function6-phosphofructokinase activity
D0005737cellular_componentcytoplasm
D0006002biological_processfructose 6-phosphate metabolic process
D0006096biological_processglycolytic process
D0016301molecular_functionkinase activity
D0046835biological_processcarbohydrate phosphorylation
D0046872molecular_functionmetal ion binding
D0047334molecular_functiondiphosphate-fructose-6-phosphate 1-phosphotransferase activity
D0061615biological_processglycolytic process through fructose-6-phosphate
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BR C 500
ChainResidue
CHIS329
CASN330
DHIS329
DASN330

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1pfk
ChainResidueDetails
ATHR142
AGLY13
AARG80
AARG192
AASP144

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1pfk
ChainResidueDetails
BTHR142
BGLY13
BARG80
BARG192
BASP144

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1pfk
ChainResidueDetails
CTHR142
CGLY13
CARG80
CARG192
CASP144

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1pfk
ChainResidueDetails
DTHR142
DGLY13
DARG80
DARG192
DASP144

site_idCSA5
Number of Residues5
DetailsAnnotated By Reference To The Literature 1pfk
ChainResidueDetails
AGLY13
ATHR142
AARG80
ALYS141
AASP144

site_idCSA6
Number of Residues5
DetailsAnnotated By Reference To The Literature 1pfk
ChainResidueDetails
BGLY13
BTHR142
BARG80
BLYS141
BASP144

site_idCSA7
Number of Residues5
DetailsAnnotated By Reference To The Literature 1pfk
ChainResidueDetails
CGLY13
CTHR142
CARG80
CLYS141
CASP144

site_idCSA8
Number of Residues5
DetailsAnnotated By Reference To The Literature 1pfk
ChainResidueDetails
DGLY13
DTHR142
DARG80
DLYS141
DASP144

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon