5IWQ
Crystal structure of aspartate aminotransferase (AspAT) from Corynebacterium glutamicum ATCC 13032
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0016740 | molecular_function | transferase activity |
| B | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0016740 | molecular_function | transferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue PLP A 501 |
| Chain | Residue |
| A | SER103 |
| A | SER256 |
| A | SER258 |
| A | LYS259 |
| A | HOH714 |
| B | TYR73 |
| A | SER104 |
| A | LEU105 |
| A | TYR142 |
| A | VAL186 |
| A | ASN191 |
| A | ASP220 |
| A | ALA222 |
| A | TYR223 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | TRP219 |
| A | ASN221 |
| A | ILE236 |
| A | ILE238 |
| A | ALA253 |
| A | PHE254 |
| A | THR255 |
| A | HOH668 |
| A | HOH677 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | GLU95 |
| A | GLN96 |
| A | VAL239 |
| A | GLU243 |
| A | ARG277 |
| A | HOH655 |
| A | HOH724 |
| A | HOH829 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | ARG13 |
| A | PHE17 |
| A | ASP20 |
| A | VAL345 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 505 |
| Chain | Residue |
| A | ARG83 |
| A | GLU95 |
| A | VAL97 |
| A | LEU98 |
| A | ARG277 |
| A | HOH686 |
| A | HOH765 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 506 |
| Chain | Residue |
| A | LYS34 |
| A | LEU35 |
| A | ASP36 |
| A | GLY372 |
| A | HOH607 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | binding site for residue PLP B 501 |
| Chain | Residue |
| A | TYR73 |
| B | SER103 |
| B | SER104 |
| B | LEU105 |
| B | TYR142 |
| B | VAL186 |
| B | ASN191 |
| B | ASP220 |
| B | ALA222 |
| B | TYR223 |
| B | SER256 |
| B | SER258 |
| B | LYS259 |
| B | FLC502 |
| B | HOH625 |
| B | HOH655 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue FLC B 502 |
| Chain | Residue |
| A | TYR73 |
| A | ILE289 |
| B | ARG39 |
| B | GLY40 |
| B | TYR142 |
| B | ARG144 |
| B | TYR223 |
| B | LYS259 |
| B | ARG394 |
| B | PLP501 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| B | GLU130 |
| B | GLU131 |
| B | THR132 |
| B | VAL133 |
| B | PHE152 |
| B | GLY153 |
| B | HOH601 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| B | GLU45 |
| B | ALA318 |
| B | HOH641 |
| B | HOH785 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 505 |
| Chain | Residue |
| B | ASP122 |
| B | VAL124 |
| B | PRO213 |
| B | HOH856 |
| B | HOH865 |
| site_id | AD3 |
| Number of Residues | 9 |
| Details | binding site for residue GOL B 506 |
| Chain | Residue |
| B | PHE189 |
| B | GLY194 |
| B | PHE195 |
| B | THR196 |
| B | PRO346 |
| B | ALA347 |
| B | HOH622 |
| B | HOH673 |
| B | HOH917 |
| site_id | AD4 |
| Number of Residues | 9 |
| Details | binding site for residue GOL B 507 |
| Chain | Residue |
| B | THR229 |
| B | ALA321 |
| B | PHE324 |
| B | LEU328 |
| B | PRO346 |
| B | HOH682 |
| B | HOH713 |
| B | HOH894 |
| B | ASP20 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2016","submissionDatabase":"PDB data bank","title":"Structural insights into a novel class of aspartate aminotransferase from Corynebacterium glutamicum.","authors":["Son H.-F.","Kim K.-J."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27355211","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of an aspartate transaminase (NCgl0237, Cgl0240) from Corynebacterium glutamicum ATCC 13032 kitasato at 1.25 A resolution.","authoringGroup":["Joint Center for Structural Genomics (JCSG)"]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2016","submissionDatabase":"PDB data bank","title":"Structural insights into a novel class of aspartate aminotransferase from Corynebacterium glutamicum.","authors":["Son H.-F.","Kim K.-J."]}}]} |
| Chain | Residue | Details |
