2BNE
The structure of E. coli UMP kinase in complex with UMP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| A | 0006225 | biological_process | UDP biosynthetic process |
| A | 0009041 | molecular_function | UMP/dUMP kinase activity |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| A | 0033862 | molecular_function | UMP kinase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0044210 | biological_process | 'de novo' CTP biosynthetic process |
| A | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| B | 0006225 | biological_process | UDP biosynthetic process |
| B | 0009041 | molecular_function | UMP/dUMP kinase activity |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016310 | biological_process | phosphorylation |
| B | 0033862 | molecular_function | UMP kinase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0044210 | biological_process | 'de novo' CTP biosynthetic process |
| B | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE U5P A1242 |
| Chain | Residue |
| A | GLY56 |
| A | ASN140 |
| A | PRO141 |
| A | PHE143 |
| A | THR144 |
| A | THR145 |
| A | HOH2015 |
| A | HOH2042 |
| A | GLY57 |
| A | GLY58 |
| A | ARG62 |
| A | GLY63 |
| A | ASP77 |
| A | GLY80 |
| A | MET81 |
| A | THR138 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE U5P B1242 |
| Chain | Residue |
| B | GLY56 |
| B | GLY57 |
| B | GLY58 |
| B | ARG62 |
| B | GLY63 |
| B | ASP77 |
| B | GLY80 |
| B | MET81 |
| B | THR84 |
| B | THR138 |
| B | ASN140 |
| B | PRO141 |
| B | PHE143 |
| B | THR144 |
| B | THR145 |
| B | HOH2023 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A1243 |
| Chain | Residue |
| A | GLN39 |
| A | LYS42 |
| A | GOL1244 |
| A | HOH2043 |
| B | GLN39 |
| B | GLU46 |
| B | GOL1244 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A1244 |
| Chain | Residue |
| A | GLN39 |
| A | GLU46 |
| A | GOL1243 |
| B | GLN39 |
| B | LYS42 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A1245 |
| Chain | Residue |
| A | VAL192 |
| A | LEU193 |
| A | GLU196 |
| A | LEU197 |
| A | VAL199 |
| A | MET200 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A1246 |
| Chain | Residue |
| A | TYR99 |
| A | VAL100 |
| A | ASN101 |
| A | ARG127 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL B1243 |
| Chain | Residue |
| A | HIS211 |
| B | ARG73 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B1244 |
| Chain | Residue |
| A | LYS195 |
| A | GOL1243 |
| B | GLN39 |
| B | GLU43 |
| B | ARG227 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B1245 |
| Chain | Residue |
| B | LYS10 |
| B | GLN50 |
| B | ARG127 |
| B | ASN129 |
| B | HOH2004 |
| B | HOH2052 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15857829, ECO:0000269|PubMed:18945668, ECO:0007744|PDB:2BND, ECO:0007744|PDB:2BNF, ECO:0007744|PDB:2V4Y |
| Chain | Residue | Details |
| A | LEU16 | |
| A | GLY58 | |
| A | ASN59 | |
| B | LEU16 | |
| B | GLY58 | |
| B | ASN59 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15857829, ECO:0007744|PDB:2BND, ECO:0007744|PDB:2BNE, ECO:0007744|PDB:2BNF |
| Chain | Residue | Details |
| A | GLY63 | |
| B | GLY63 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15857829, ECO:0000269|PubMed:18945668, ECO:0007744|PDB:2BNE, ECO:0007744|PDB:2BNF, ECO:0007744|PDB:2V4Y |
| Chain | Residue | Details |
| A | HIS78 | |
| B | HIS78 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15857829, ECO:0000269|PubMed:18945668, ECO:0007744|PDB:2BND, ECO:0007744|PDB:2BNE, ECO:0007744|PDB:2BNF, ECO:0007744|PDB:2V4Y |
| Chain | Residue | Details |
| A | GLY139 | |
| B | GLY139 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS166 | |
| A | THR172 | |
| A | PRO175 | |
| B | LYS166 | |
| B | THR172 | |
| B | PRO175 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18945668, ECO:0007744|PDB:2V4Y |
| Chain | Residue | Details |
| A | ASP93 | |
| A | ALA102 | |
| B | ASP93 | |
| B | ALA102 |
