3UMO
Crystal structure of the Phosphofructokinase-2 from Escherichia coli in complex with Potassium
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003872 | molecular_function | 6-phosphofructokinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006096 | biological_process | glycolytic process |
| A | 0006974 | biological_process | DNA damage response |
| A | 0009024 | molecular_function | tagatose-6-phosphate kinase activity |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| A | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0061615 | biological_process | glycolytic process through fructose-6-phosphate |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003872 | molecular_function | 6-phosphofructokinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006096 | biological_process | glycolytic process |
| B | 0006974 | biological_process | DNA damage response |
| B | 0009024 | molecular_function | tagatose-6-phosphate kinase activity |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016310 | biological_process | phosphorylation |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| B | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0061615 | biological_process | glycolytic process through fructose-6-phosphate |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 310 |
| Chain | Residue |
| A | ATP313 |
| A | HOH532 |
| A | HOH533 |
| A | HOH535 |
| B | HOH534 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 311 |
| Chain | Residue |
| A | ATP313 |
| A | HOH686 |
| B | ATP312 |
| B | HOH531 |
| site_id | AC3 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE ATP A 313 |
| Chain | Residue |
| A | LYS185 |
| A | ASN187 |
| A | SER224 |
| A | LEU225 |
| A | GLY226 |
| A | PRO227 |
| A | GLY229 |
| A | THR251 |
| A | ALA254 |
| A | GLY255 |
| A | MET258 |
| A | VAL280 |
| A | GLY283 |
| A | SER284 |
| A | THR287 |
| A | MG310 |
| A | MG311 |
| A | HOH320 |
| A | HOH323 |
| A | HOH326 |
| A | HOH360 |
| A | HOH516 |
| A | HOH518 |
| A | HOH532 |
| A | HOH533 |
| A | HOH535 |
| A | HOH649 |
| A | HOH686 |
| B | LYS27 |
| B | ATP312 |
| B | HOH531 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 314 |
| Chain | Residue |
| A | SER250 |
| A | VAL252 |
| A | ALA286 |
| A | ASN289 |
| A | GLY291 |
| A | ARG293 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 312 |
| Chain | Residue |
| A | ATP315 |
| A | HOH536 |
| B | ATP313 |
| B | HOH669 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ATP A 315 |
| Chain | Residue |
| A | TYR23 |
| A | PRO24 |
| A | GLY26 |
| A | LYS27 |
| A | GLU102 |
| A | MG312 |
| A | HOH339 |
| A | HOH344 |
| A | HOH348 |
| A | HOH382 |
| A | HOH437 |
| A | HOH514 |
| A | HOH529 |
| A | HOH536 |
| A | HOH682 |
| B | ASN187 |
| B | LYS189 |
| B | GLY226 |
| B | PRO227 |
| B | THR251 |
| B | ATP313 |
| B | HOH452 |
| site_id | AC7 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ATP B 312 |
| Chain | Residue |
| A | ASN187 |
| A | LYS189 |
| A | GLY226 |
| A | THR251 |
| A | MG311 |
| A | ATP313 |
| A | HOH358 |
| A | HOH547 |
| B | TYR23 |
| B | GLY26 |
| B | LYS27 |
| B | GLU102 |
| B | HOH386 |
| B | HOH418 |
| B | HOH423 |
| B | HOH434 |
| B | HOH463 |
| B | HOH480 |
| B | HOH508 |
| B | HOH531 |
| B | HOH534 |
| B | HOH582 |
| B | HOH591 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 311 |
| Chain | Residue |
| B | HOH342 |
| A | HOH339 |
| B | HOH310 |
| B | ATP313 |
| B | HOH318 |
| site_id | AC9 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE ATP B 313 |
| Chain | Residue |
| A | LYS27 |
| A | MG312 |
| A | ATP315 |
| A | HOH339 |
| A | HOH536 |
| B | LYS185 |
| B | ASN187 |
| B | SER224 |
| B | LEU225 |
| B | GLY226 |
| B | PRO227 |
| B | GLY229 |
| B | ALA254 |
| B | GLY255 |
| B | MET258 |
| B | VAL280 |
| B | GLY283 |
| B | SER284 |
| B | THR287 |
| B | HOH310 |
| B | MG311 |
| B | HOH318 |
| B | HOH325 |
| B | HOH342 |
| B | HOH344 |
| B | HOH352 |
| B | HOH412 |
| B | HOH441 |
| B | HOH548 |
| B | HOH557 |
| B | HOH669 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 314 |
| Chain | Residue |
| B | SER250 |
| B | VAL252 |
| B | ALA286 |
| B | ASN289 |
| B | GLY291 |
| B | ARG293 |
Functional Information from PROSITE/UniProt
| site_id | PS00583 |
| Number of Residues | 25 |
| Details | PFKB_KINASES_1 pfkB family of carbohydrate kinases signature 1. GGgGiNVAraIaHLGgsataifpaG |
| Chain | Residue | Details |
| A | GLY38-GLY62 |
| site_id | PS00584 |
| Number of Residues | 14 |
| Details | PFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. STvGAGDsmvGAMT |
| Chain | Residue | Details |
| A | SER250-THR263 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP256 | |
| B | ASP256 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | SER12 | |
| B | ASP256 | |
| A | GLY39 | |
| A | ARG90 | |
| A | SER139 | |
| A | ASP256 | |
| B | SER12 | |
| B | GLY39 | |
| B | ARG90 | |
| B | SER139 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18762190, ECO:0007744|PDB:3CQD |
| Chain | Residue | Details |
| A | LYS27 | |
| B | LYS27 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:18762190, ECO:0000269|PubMed:23823238, ECO:0000269|Ref.10, ECO:0000269|Ref.11, ECO:0007744|PDB:3CQD |
| Chain | Residue | Details |
| A | LYS185 | |
| B | SER284 | |
| A | SER224 | |
| A | SER248 | |
| A | VAL280 | |
| A | SER284 | |
| B | LYS185 | |
| B | SER224 | |
| B | SER248 | |
| B | VAL280 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:18762190, ECO:0007744|PDB:3CQD |
| Chain | Residue | Details |
| A | ASN187 | |
| B | ASN187 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| A | GLU190 | |
| B | GLU190 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23823238 |
| Chain | Residue | Details |
| A | SER250 | |
| B | ASN289 | |
| B | GLY291 | |
| B | ARG293 | |
| A | VAL252 | |
| A | ALA286 | |
| A | ASN289 | |
| A | GLY291 | |
| A | ARG293 | |
| B | SER250 | |
| B | VAL252 | |
| B | ALA286 |
