3BF3
Type III pantothenate kinase from Thermotoga maritima complexed with product phosphopantothenate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0043169 | molecular_function | cation binding |
| A | 0046872 | molecular_function | metal ion 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 | 0043169 | molecular_function | cation binding |
| B | 0046872 | molecular_function | metal ion 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 | 0043169 | molecular_function | cation binding |
| C | 0046872 | molecular_function | metal ion 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 | 0043169 | molecular_function | cation binding |
| D | 0046872 | molecular_function | metal ion 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 | 0043169 | molecular_function | cation binding |
| E | 0046872 | molecular_function | metal ion 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 | 0043169 | molecular_function | cation binding |
| F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 247 |
| Chain | Residue |
| A | HIS42 |
| A | HOH392 |
| D | HIS42 |
| D | HOH432 |
| F | HIS42 |
| F | HOH504 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 247 |
| Chain | Residue |
| C | HOH333 |
| E | HIS42 |
| E | HOH377 |
| B | HIS42 |
| B | HOH551 |
| C | HIS42 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PAZ A 248 |
| Chain | Residue |
| A | ASN9 |
| A | GLU101 |
| A | GLY103 |
| A | ASP105 |
| A | ARG106 |
| A | THR128 |
| A | ALA129 |
| A | HOH256 |
| A | HOH349 |
| A | HOH480 |
| B | LYS162 |
| B | LEU163 |
| B | THR179 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PAZ E 247 |
| Chain | Residue |
| E | ASN9 |
| E | GLU101 |
| E | GLY103 |
| E | ASP105 |
| E | ARG106 |
| E | THR128 |
| E | ALA129 |
| E | THR131 |
| E | HOH250 |
| E | HOH297 |
| E | HOH304 |
| F | LYS162 |
| F | LEU163 |
| F | THR179 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PAZ B 248 |
| Chain | Residue |
| A | LYS162 |
| A | LEU163 |
| A | THR179 |
| B | ASN9 |
| B | GLU101 |
| B | GLY103 |
| B | ASP105 |
| B | ARG106 |
| B | THR128 |
| B | ALA129 |
| B | HOH257 |
| B | HOH297 |
| B | HOH401 |
| B | HOH429 |
| B | HOH512 |
| B | HOH543 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PAZ C 247 |
| Chain | Residue |
| C | ASN9 |
| C | GLU101 |
| C | GLY103 |
| C | ASP105 |
| C | ARG106 |
| C | THR128 |
| C | ALA129 |
| C | THR131 |
| C | HOH251 |
| C | HOH306 |
| C | HOH468 |
| D | THR160 |
| D | LYS162 |
| D | LEU163 |
| D | THR179 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PAZ D 247 |
| Chain | Residue |
| C | LYS162 |
| C | LEU163 |
| C | THR179 |
| D | ASN9 |
| D | GLU101 |
| D | GLY103 |
| D | ASP105 |
| D | ARG106 |
| D | THR128 |
| D | ALA129 |
| D | THR131 |
| D | HOH250 |
| D | HOH360 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PAZ F 247 |
| Chain | Residue |
| E | LYS162 |
| E | LEU163 |
| E | THR179 |
| F | ASN9 |
| F | GLU101 |
| F | GLY103 |
| F | ASP105 |
| F | ARG106 |
| F | THR128 |
| F | ALA129 |
| F | THR131 |
| F | HOH248 |
| F | HOH358 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255 |
| Chain | Residue | Details |
| A | ASP105 | |
| B | ASP105 | |
| C | ASP105 | |
| D | ASP105 | |
| E | ASP105 | |
| F | ASP105 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP6 | |
| D | ASP6 | |
| D | GLY103 | |
| D | THR179 | |
| E | ASP6 | |
| E | GLY103 | |
| E | THR179 | |
| F | ASP6 | |
| F | GLY103 | |
| F | THR179 | |
| A | GLY103 | |
| A | THR179 | |
| B | ASP6 | |
| B | GLY103 | |
| B | THR179 | |
| C | ASP6 | |
| C | GLY103 | |
| C | THR179 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| A | ASP125 | |
| E | THR128 | |
| F | ASP125 | |
| F | THR128 | |
| A | THR128 | |
| B | ASP125 | |
| B | THR128 | |
| C | ASP125 | |
| C | THR128 | |
| D | ASP125 | |
| D | THR128 | |
| E | ASP125 |
