2BIF
6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE H256A MUTANT WITH F6P IN PHOSPHATASE ACTIVE SITE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003873 | molecular_function | 6-phosphofructo-2-kinase activity |
| A | 0004331 | molecular_function | fructose-2,6-bisphosphate 2-phosphatase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006000 | biological_process | fructose metabolic process |
| A | 0006003 | biological_process | fructose 2,6-bisphosphate metabolic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046835 | biological_process | carbohydrate phosphorylation |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003873 | molecular_function | 6-phosphofructo-2-kinase activity |
| B | 0004331 | molecular_function | fructose-2,6-bisphosphate 2-phosphatase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006000 | biological_process | fructose metabolic process |
| B | 0006003 | biological_process | fructose 2,6-bisphosphate metabolic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046835 | biological_process | carbohydrate phosphorylation |
Functional Information from PDB Data
| site_id | S1 |
| Number of Residues | 16 |
| Details | WALKER-A MOTIF (GXXGXGKT), PART OF THE CLASSICAL MONONUCLEOTIDE BINDING MOTIF. |
| Chain | Residue |
| A | GLY45 |
| B | LEU46 |
| B | PRO47 |
| B | ALA48 |
| B | ARG49 |
| B | GLY50 |
| B | LYS51 |
| B | THR52 |
| A | LEU46 |
| A | PRO47 |
| A | ALA48 |
| A | ARG49 |
| A | GLY50 |
| A | LYS51 |
| A | THR52 |
| B | GLY45 |
| site_id | S2 |
| Number of Residues | 10 |
| Details | WALKER-B MOTIF (ZZZZD, Z=HYDROPHOBIC), PART OF THE CLASSICAL MONONUCLEOTIDE BINDING MOTIF. ASP 128 SERVES AS A LIGAND TO THE MG OF MG-ATP. |
| Chain | Residue |
| A | VAL124 |
| A | ALA125 |
| A | VAL126 |
| A | PHE127 |
| A | ASP128 |
| B | VAL124 |
| B | ALA125 |
| B | VAL126 |
| B | PHE127 |
| B | ASP128 |
| site_id | S3 |
| Number of Residues | 6 |
| Details | CATALYTIC TRIAD FOR THE FRUCTOSE-2,6-BISPHOSPHATASE REACTION. |
| Chain | Residue |
| A | ALA256 |
| A | GLU325 |
| A | HIS390 |
| B | ALA256 |
| B | GLU325 |
| B | HIS390 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255 |
| Chain | Residue | Details |
| A | ASP128 | |
| A | CYS158 | |
| B | ASP128 | |
| B | CYS158 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Tele-phosphohistidine intermediate => ECO:0000269|PubMed:9890980 |
| Chain | Residue | Details |
| A | ALA256 | |
| B | ALA256 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:9890980 |
| Chain | Residue | Details |
| A | GLU325 | |
| B | GLU325 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8805587 |
| Chain | Residue | Details |
| A | GLY45 | |
| A | ASN167 | |
| A | TYR427 | |
| B | GLY45 | |
| B | ASN167 | |
| B | TYR427 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 22 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:9890980 |
| Chain | Residue | Details |
| A | ARG78 | |
| A | GLN391 | |
| A | ARG395 | |
| B | ARG78 | |
| B | THR130 | |
| B | ARG136 | |
| B | TYR197 | |
| B | GLY268 | |
| B | TYR336 | |
| B | ARG350 | |
| B | LYS354 | |
| A | THR130 | |
| B | TYR365 | |
| B | GLN391 | |
| B | ARG395 | |
| A | ARG136 | |
| A | TYR197 | |
| A | GLY268 | |
| A | TYR336 | |
| A | ARG350 | |
| A | LYS354 | |
| A | TYR365 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q16875 |
| Chain | Residue | Details |
| A | ARG102 | |
| B | ARG255 | |
| B | ASN262 | |
| B | ARG305 | |
| A | LYS172 | |
| A | ARG193 | |
| A | ARG255 | |
| A | ASN262 | |
| A | ARG305 | |
| B | ARG102 | |
| B | LYS172 | |
| B | ARG193 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P07953 |
| Chain | Residue | Details |
| A | PHE347 | |
| B | PHE347 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00950 |
| Chain | Residue | Details |
| A | HIS390 | |
| B | HIS390 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by PKC => ECO:0000255 |
| Chain | Residue | Details |
| A | SER28 | |
| B | SER28 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine; by PKC => ECO:0000255 |
| Chain | Residue | Details |
| A | THR443 | |
| B | THR443 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 2168419, 6304027, 6319392, 1326547, 9890980, 11123954 |
| Chain | Residue | Details |
| A | GLU325 | |
| A | ASN262 | |
| A | HIS390 | |
| A | ARG255 | |
| A | ARG305 | |
| A | ALA256 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 2168419, 6304027, 6319392, 1326547, 9890980, 11123954 |
| Chain | Residue | Details |
| B | GLU325 | |
| B | ASN262 | |
| B | HIS390 | |
| B | ARG255 | |
| B | ARG305 | |
| B | ALA256 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 810 |
| Chain | Residue | Details |
| A | ARG255 | electrostatic stabiliser |
| A | ALA256 | covalently attached, nucleofuge, nucleophile |
| A | ASN262 | electrostatic stabiliser |
| A | ARG305 | electrostatic stabiliser |
| A | GLU325 | activator, proton acceptor, proton donor |
| A | HIS390 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 810 |
| Chain | Residue | Details |
| B | ARG255 | electrostatic stabiliser |
| B | ALA256 | covalently attached, nucleofuge, nucleophile |
| B | ASN262 | electrostatic stabiliser |
| B | ARG305 | electrostatic stabiliser |
| B | GLU325 | activator, proton acceptor, proton donor |
| B | HIS390 | electrostatic stabiliser |
