3B1R
Structure of Burkholderia thailandensis nucleoside kinase (BthNK) in complex with AMP-Mg-AMP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0016301 | molecular_function | kinase activity |
| C | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0016301 | molecular_function | kinase activity |
| D | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0016301 | molecular_function | kinase activity |
| E | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0016301 | molecular_function | kinase activity |
| F | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE AMP A 501 |
| Chain | Residue |
| A | SER8 |
| A | PRO143 |
| A | GLN169 |
| A | GLY250 |
| A | ASP253 |
| A | HOH313 |
| A | HOH315 |
| A | HOH317 |
| A | HOH322 |
| A | HOH348 |
| A | HOH409 |
| A | ALA10 |
| A | MG503 |
| D | SER36 |
| A | ASP12 |
| A | GLY48 |
| A | CYS49 |
| A | ASN52 |
| A | GLN113 |
| A | PHE117 |
| A | MET122 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE AMP A 502 |
| Chain | Residue |
| A | ASN111 |
| A | THR220 |
| A | ARG221 |
| A | GLY222 |
| A | GLU223 |
| A | GLY225 |
| A | VAL240 |
| A | GLY252 |
| A | PHE255 |
| A | SER277 |
| A | GLY280 |
| A | ILE284 |
| A | HOH325 |
| A | HOH483 |
| A | HOH587 |
| A | HOH763 |
| A | HOH780 |
| D | HIS31 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 503 |
| Chain | Residue |
| A | HOH313 |
| A | HOH314 |
| A | HOH315 |
| A | HOH316 |
| A | HOH317 |
| A | AMP501 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE AMP B 501 |
| Chain | Residue |
| B | SER8 |
| B | ALA10 |
| B | ASP12 |
| B | GLY48 |
| B | CYS49 |
| B | ASN52 |
| B | GLN113 |
| B | PHE117 |
| B | MET122 |
| B | PRO143 |
| B | GLN169 |
| B | GLY250 |
| B | ASP253 |
| B | HOH314 |
| B | HOH315 |
| B | HOH316 |
| B | HOH317 |
| B | HOH319 |
| B | HOH361 |
| B | MG503 |
| B | HOH868 |
| E | SER36 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE AMP B 502 |
| Chain | Residue |
| B | ASN111 |
| B | THR220 |
| B | ARG221 |
| B | GLY222 |
| B | GLU223 |
| B | GLY225 |
| B | VAL240 |
| B | CYS251 |
| B | GLY252 |
| B | SER277 |
| B | GLY280 |
| B | ILE284 |
| B | HOH318 |
| B | HOH321 |
| B | HOH325 |
| B | HOH364 |
| B | HOH638 |
| B | HOH751 |
| E | HIS31 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 503 |
| Chain | Residue |
| B | HOH313 |
| B | HOH314 |
| B | HOH315 |
| B | HOH316 |
| B | HOH317 |
| B | AMP501 |
| site_id | AC7 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE AMP C 501 |
| Chain | Residue |
| C | GLN113 |
| C | PHE117 |
| C | MET122 |
| C | PRO143 |
| C | GLN169 |
| C | GLY250 |
| C | ASP253 |
| C | HOH313 |
| C | HOH315 |
| C | HOH317 |
| C | HOH354 |
| C | MG503 |
| C | HOH697 |
| F | SER36 |
| C | SER8 |
| C | ALA10 |
| C | ASP12 |
| C | GLY47 |
| C | GLY48 |
| C | CYS49 |
| C | ASN52 |
| site_id | AC8 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE AMP C 502 |
| Chain | Residue |
| C | ASN111 |
| C | THR220 |
| C | ARG221 |
| C | GLY222 |
| C | GLY225 |
| C | VAL240 |
| C | CYS251 |
| C | GLY252 |
| C | PHE255 |
| C | SER277 |
| C | GLY280 |
| C | ILE284 |
| C | HOH318 |
| C | HOH350 |
| C | HOH421 |
| C | HOH846 |
| F | HIS31 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 503 |
| Chain | Residue |
| C | HOH313 |
| C | HOH314 |
| C | HOH315 |
| C | HOH316 |
| C | HOH317 |
| C | AMP501 |
| site_id | BC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE AMP D 501 |
| Chain | Residue |
| A | SER36 |
| D | SER8 |
| D | ALA10 |
| D | ASP12 |
| D | GLY47 |
| D | GLY48 |
| D | CYS49 |
| D | ASN52 |
| D | GLN113 |
| D | PHE117 |
| D | GLN169 |
| D | GLY250 |
| D | ASP253 |
| D | HOH316 |
| D | HOH317 |
| D | HOH318 |
| D | MG503 |
| D | HOH605 |
| D | HOH951 |
| site_id | BC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE AMP D 502 |
| Chain | Residue |
| A | HIS31 |
| D | ASN111 |
| D | THR220 |
| D | GLY222 |
| D | GLY225 |
| D | VAL240 |
| D | CYS251 |
| D | GLY252 |
| D | PHE255 |
| D | SER277 |
| D | GLY280 |
| D | ILE284 |
| D | HOH321 |
| D | HOH332 |
| D | HOH463 |
| D | HOH578 |
| D | HOH665 |
| D | HOH768 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 503 |
| Chain | Residue |
| D | HOH314 |
| D | HOH316 |
| D | HOH317 |
| D | HOH318 |
| D | AMP501 |
| D | HOH951 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 313 |
| Chain | Residue |
| D | GLU184 |
| D | ARG213 |
| D | HOH1082 |
| D | HOH1083 |
| D | HOH1085 |
| D | HOH1086 |
| site_id | BC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE AMP E 501 |
| Chain | Residue |
| B | SER36 |
| E | SER8 |
| E | ALA10 |
| E | ASP12 |
| E | GLY47 |
| E | GLY48 |
| E | CYS49 |
| E | ASN52 |
| E | GLN113 |
| E | PHE117 |
| E | MET122 |
| E | PRO143 |
| E | GLN169 |
| E | GLY250 |
| E | ASP253 |
| E | HOH318 |
| E | HOH329 |
| E | HOH353 |
| E | MG503 |
| site_id | BC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE AMP E 502 |
| Chain | Residue |
| B | HIS31 |
| E | ASN111 |
| E | THR220 |
| E | ARG221 |
| E | GLY222 |
| E | GLU223 |
| E | GLY225 |
| E | VAL240 |
| E | SER277 |
| E | GLY280 |
| E | ILE284 |
| E | HOH322 |
| E | HOH324 |
| E | HOH331 |
| E | HOH332 |
| E | HOH333 |
| E | HOH376 |
| E | HOH392 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG E 503 |
| Chain | Residue |
| E | GLN169 |
| E | HOH314 |
| E | HOH315 |
| E | HOH318 |
| E | HOH319 |
| E | HOH320 |
| E | AMP501 |
| site_id | BC8 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE AMP F 501 |
| Chain | Residue |
| C | SER36 |
| F | SER8 |
| F | ASP12 |
| F | GLY48 |
| F | CYS49 |
| F | ASN52 |
| F | GLN113 |
| F | PHE117 |
| F | MET122 |
| F | PRO143 |
| F | GLN169 |
| F | GLY250 |
| F | ASP253 |
| F | HOH313 |
| F | HOH315 |
| F | HOH317 |
| F | HOH318 |
| F | HOH319 |
| F | HOH328 |
| F | HOH381 |
| F | MG503 |
| site_id | BC9 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE AMP F 502 |
| Chain | Residue |
| C | HIS31 |
| F | ASN111 |
| F | THR220 |
| F | GLY222 |
| F | GLU223 |
| F | GLY225 |
| F | VAL240 |
| F | GLY252 |
| F | SER277 |
| F | GLY280 |
| F | HOH322 |
| F | HOH329 |
| F | HOH352 |
| F | HOH447 |
| F | HOH761 |
| F | HOH876 |
| F | HOH969 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG F 503 |
| Chain | Residue |
| F | HOH313 |
| F | HOH315 |
| F | HOH316 |
| F | HOH317 |
| F | HOH318 |
| F | AMP501 |
Functional Information from PROSITE/UniProt
| site_id | PS00583 |
| Number of Residues | 25 |
| Details | PFKB_KINASES_1 pfkB family of carbohydrate kinases signature 1. GGcAgNIAyaLnLLGgdarmmgtlG |
| Chain | Residue | Details |
| A | GLY47-GLY71 |
