3BF1
Type III pantothenate kinase from Thermotoga maritima complexed with pantothenate and ADP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004594 | molecular_function | pantothenate kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0015937 | biological_process | coenzyme A biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0043169 | molecular_function | cation binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004594 | molecular_function | pantothenate kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0015937 | biological_process | coenzyme A biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0043169 | molecular_function | cation binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004594 | molecular_function | pantothenate kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0015937 | biological_process | coenzyme A biosynthetic process |
| C | 0016301 | molecular_function | kinase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0043169 | molecular_function | cation binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004594 | molecular_function | pantothenate kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0015937 | biological_process | coenzyme A biosynthetic process |
| D | 0016301 | molecular_function | kinase activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0043169 | molecular_function | cation binding |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0004594 | molecular_function | pantothenate kinase activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0015937 | biological_process | coenzyme A biosynthetic process |
| E | 0016301 | molecular_function | kinase activity |
| E | 0016740 | molecular_function | transferase activity |
| E | 0043169 | molecular_function | cation binding |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0004594 | molecular_function | pantothenate kinase activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0015937 | biological_process | coenzyme A biosynthetic process |
| F | 0016301 | molecular_function | kinase activity |
| F | 0016740 | molecular_function | transferase activity |
| F | 0043169 | molecular_function | cation binding |
| F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ADP A 247 |
| Chain | Residue |
| A | THR10 |
| F | PHE33 |
| A | HIS11 |
| A | ARG27 |
| A | GLY127 |
| A | THR128 |
| A | PHE150 |
| A | GLN217 |
| A | HOH277 |
| A | HOH302 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADP B 247 |
| Chain | Residue |
| B | THR10 |
| B | HIS11 |
| B | ARG27 |
| B | GLY127 |
| B | THR128 |
| B | PHE150 |
| B | GLN217 |
| B | HOH258 |
| B | HOH284 |
| B | HOH285 |
| B | HOH307 |
| B | HOH308 |
| C | PHE33 |
| C | THR65 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ADP C 247 |
| Chain | Residue |
| C | THR10 |
| C | HIS11 |
| C | ARG27 |
| C | GLY127 |
| C | THR128 |
| C | PHE150 |
| C | GLN217 |
| C | HOH256 |
| C | HOH267 |
| C | HOH290 |
| E | PHE33 |
| E | THR65 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ADP D 247 |
| Chain | Residue |
| A | PHE33 |
| D | THR10 |
| D | HIS11 |
| D | GLY127 |
| D | THR128 |
| D | PHE150 |
| D | GLN217 |
| D | HOH260 |
| D | HOH269 |
| D | HOH285 |
| D | HOH290 |
| D | HOH358 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ADP E 247 |
| Chain | Residue |
| B | PHE33 |
| E | THR10 |
| E | HIS11 |
| E | ARG27 |
| E | GLY127 |
| E | THR128 |
| E | PHE150 |
| E | GLN217 |
| E | HOH257 |
| E | HOH321 |
| E | HOH333 |
| E | HOH355 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ADP F 247 |
| Chain | Residue |
| D | PHE33 |
| F | THR10 |
| F | HIS11 |
| F | ARG27 |
| F | GLY127 |
| F | THR128 |
| F | PHE150 |
| F | GLY216 |
| F | GLN217 |
| F | HOH255 |
| F | HOH259 |
| F | HOH263 |
| F | HOH295 |
| F | HOH300 |
| F | HOH331 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PAU A 248 |
| Chain | Residue |
| A | GLU101 |
| A | GLY103 |
| A | ASP105 |
| A | ARG106 |
| A | HOH255 |
| B | LYS162 |
| B | LEU163 |
| B | THR179 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PAU B 248 |
| Chain | Residue |
| A | LYS162 |
| A | LEU163 |
| A | THR179 |
| B | GLU101 |
| B | GLY103 |
| B | ASP105 |
| B | ARG106 |
| B | HOH273 |
| B | HOH335 |
| B | HOH342 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PAU C 248 |
| Chain | Residue |
| D | LYS162 |
| D | LEU163 |
| D | THR179 |
| C | GLU101 |
| C | GLY103 |
| C | ASP105 |
| C | ARG106 |
| C | HOH258 |
| D | THR160 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PAU D 248 |
| Chain | Residue |
| C | LYS162 |
| C | LEU163 |
| C | THR179 |
| D | GLU101 |
| D | GLY103 |
| D | ASP105 |
| D | ARG106 |
| D | HOH258 |
| D | HOH335 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PAU E 248 |
| Chain | Residue |
| E | GLU101 |
| E | GLY103 |
| E | ASP105 |
| E | ARG106 |
| E | HOH270 |
| F | LYS162 |
| F | LEU163 |
| F | THR179 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PAU F 248 |
| Chain | Residue |
| E | LYS162 |
| E | THR179 |
| F | GLU101 |
| F | GLY103 |
| F | ASP105 |
| F | ARG106 |
| F | HOH252 |
| F | HOH300 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 66 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
