3AB2
Crystal structure of aspartate kinase from Corynebacterium glutamicum in complex with threonine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004072 | molecular_function | aspartate kinase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009088 | biological_process | L-threonine biosynthetic process |
| A | 0009089 | biological_process | obsolete L-lysine biosynthetic process via diaminopimelate |
| A | 0009090 | biological_process | L-homoserine biosynthetic process |
| C | 0004072 | molecular_function | aspartate kinase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0009088 | biological_process | L-threonine biosynthetic process |
| C | 0009089 | biological_process | obsolete L-lysine biosynthetic process via diaminopimelate |
| C | 0009090 | biological_process | L-homoserine biosynthetic process |
| E | 0004072 | molecular_function | aspartate kinase activity |
| E | 0005829 | cellular_component | cytosol |
| E | 0008652 | biological_process | amino acid biosynthetic process |
| E | 0009088 | biological_process | L-threonine biosynthetic process |
| E | 0009089 | biological_process | obsolete L-lysine biosynthetic process via diaminopimelate |
| E | 0009090 | biological_process | L-homoserine biosynthetic process |
| G | 0004072 | molecular_function | aspartate kinase activity |
| G | 0005829 | cellular_component | cytosol |
| G | 0008652 | biological_process | amino acid biosynthetic process |
| G | 0009088 | biological_process | L-threonine biosynthetic process |
| G | 0009089 | biological_process | obsolete L-lysine biosynthetic process via diaminopimelate |
| G | 0009090 | biological_process | L-homoserine biosynthetic process |
| I | 0004072 | molecular_function | aspartate kinase activity |
| I | 0005829 | cellular_component | cytosol |
| I | 0008652 | biological_process | amino acid biosynthetic process |
| I | 0009088 | biological_process | L-threonine biosynthetic process |
| I | 0009089 | biological_process | obsolete L-lysine biosynthetic process via diaminopimelate |
| I | 0009090 | biological_process | L-homoserine biosynthetic process |
| K | 0004072 | molecular_function | aspartate kinase activity |
| K | 0005829 | cellular_component | cytosol |
| K | 0008652 | biological_process | amino acid biosynthetic process |
| K | 0009088 | biological_process | L-threonine biosynthetic process |
| K | 0009089 | biological_process | obsolete L-lysine biosynthetic process via diaminopimelate |
| K | 0009090 | biological_process | L-homoserine biosynthetic process |
| M | 0004072 | molecular_function | aspartate kinase activity |
| M | 0005829 | cellular_component | cytosol |
| M | 0008652 | biological_process | amino acid biosynthetic process |
| M | 0009088 | biological_process | L-threonine biosynthetic process |
| M | 0009089 | biological_process | obsolete L-lysine biosynthetic process via diaminopimelate |
| M | 0009090 | biological_process | L-homoserine biosynthetic process |
| O | 0004072 | molecular_function | aspartate kinase activity |
| O | 0005829 | cellular_component | cytosol |
| O | 0008652 | biological_process | amino acid biosynthetic process |
| O | 0009088 | biological_process | L-threonine biosynthetic process |
| O | 0009089 | biological_process | obsolete L-lysine biosynthetic process via diaminopimelate |
| O | 0009090 | biological_process | L-homoserine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE THR A 501 |
| Chain | Residue |
| A | ASP274 |
| A | LYS275 |
| A | GLY277 |
| A | GLU278 |
| A | ALA279 |
| A | GLN298 |
| B | ASN125 |
| B | ILE126 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE THR B 501 |
| Chain | Residue |
| A | ILE375 |
| B | ASP25 |
| B | LYS26 |
| B | PRO27 |
| B | GLY28 |
| B | GLU29 |
| B | ALA30 |
| B | GLN49 |
| B | HOH230 |
| A | ASN374 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE THR C 501 |
| Chain | Residue |
| C | ASP274 |
| C | LYS275 |
| C | PRO276 |
| C | GLY277 |
| C | GLU278 |
| C | ALA279 |
| C | GLN298 |
| D | ILE126 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE THR D 501 |
| Chain | Residue |
| C | ASN374 |
| C | ILE375 |
| D | ASP25 |
| D | LYS26 |
| D | GLY28 |
| D | GLU29 |
| D | ALA30 |
| D | GLN49 |
| D | HOH221 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE THR E 501 |
| Chain | Residue |
| E | ASP274 |
| E | LYS275 |
| E | PRO276 |
| E | GLY277 |
| E | GLU278 |
| E | ALA279 |
| E | GLN298 |
| E | THR308 |
| E | HOH513 |
| F | ASN125 |
| F | ILE126 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE THR F 501 |
| Chain | Residue |
| E | ASN374 |
| E | ILE375 |
| E | HOH524 |
| F | SER24 |
| F | ASP25 |
| F | LYS26 |
| F | GLY28 |
| F | GLU29 |
| F | ALA30 |
| F | GLN49 |
| F | HOH220 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE THR G 501 |
| Chain | Residue |
| G | ASP274 |
| G | LYS275 |
| G | GLY277 |
| G | GLU278 |
| G | ALA279 |
| G | GLN298 |
| H | ASN125 |
| H | ILE126 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE THR H 501 |
| Chain | Residue |
| G | ASN374 |
| G | ILE375 |
| H | ILE23 |
| H | ASP25 |
| H | LYS26 |
| H | GLY28 |
| H | GLU29 |
| H | ALA30 |
| H | GLN49 |
| H | THR59 |
| H | HOH218 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE THR J 501 |
| Chain | Residue |
| I | ASN374 |
| I | ILE375 |
| J | ASP25 |
| J | LYS26 |
| J | PRO27 |
| J | GLY28 |
| J | GLU29 |
| J | ALA30 |
| J | GLN49 |
| site_id | BC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE THR K 501 |
| Chain | Residue |
| K | ASP274 |
| K | LYS275 |
| K | GLY277 |
| K | GLU278 |
| K | ALA279 |
| K | GLN298 |
| K | THR308 |
| K | ILE310 |
| K | HOH518 |
| L | ASN125 |
| L | ILE126 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE THR L 501 |
| Chain | Residue |
| L | LYS26 |
| L | GLY28 |
| L | GLU29 |
| L | ALA30 |
| L | GLN49 |
| L | HOH222 |
| K | ASN374 |
| K | ILE375 |
| L | ASP25 |
| site_id | BC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE THR M 501 |
| Chain | Residue |
| M | ILE272 |
| M | ASP274 |
| M | LYS275 |
| M | PRO276 |
| M | GLY277 |
| M | GLU278 |
| M | ALA279 |
| M | GLN298 |
| N | ASN125 |
| N | ILE126 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE THR N 501 |
| Chain | Residue |
| M | ASN374 |
| M | ILE375 |
| N | ASP25 |
| N | LYS26 |
| N | GLY28 |
| N | GLU29 |
| N | ALA30 |
| N | GLN49 |
| N | HOH224 |
| site_id | BC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE THR O 501 |
| Chain | Residue |
| O | ASP274 |
| O | LYS275 |
| O | GLY277 |
| O | GLU278 |
| O | ALA279 |
| O | GLN298 |
| O | HOH511 |
| O | HOH522 |
| P | ASN125 |
| P | ILE126 |
| site_id | BC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE THR P 501 |
| Chain | Residue |
| O | ASN374 |
| O | ILE375 |
| P | SER24 |
| P | ASP25 |
| P | LYS26 |
| P | GLY28 |
| P | GLU29 |
| P | ALA30 |
| P | GLN49 |
Functional Information from PROSITE/UniProt
| site_id | PS00324 |
| Number of Residues | 9 |
| Details | ASPARTOKINASE Aspartokinase signature. VqKYGGSSL |
| Chain | Residue | Details |
| A | VAL5-LEU13 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 178 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 216 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Site: {"description":"Contribution to the catalysis","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 684 |
| Details | Domain: {"description":"ACT 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01007","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






