5HXX
Crystal structure of AspAT from Corynebacterium glutamicum
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 | 16 |
| Details | binding site for residue PMP A 501 |
| Chain | Residue |
| A | SER103 |
| A | SER256 |
| A | SER258 |
| A | LYS259 |
| A | AKG502 |
| A | HOH625 |
| A | HOH745 |
| 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 AKG A 502 |
| Chain | Residue |
| A | GLY40 |
| A | TYR142 |
| A | ARG144 |
| A | LYS259 |
| A | PHE351 |
| A | PMP501 |
| A | HOH726 |
| A | HOH817 |
| B | TYR73 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | ARG13 |
| A | PHE17 |
| A | ASP20 |
| A | VAL345 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| B | PHE189 |
| B | GLY194 |
| B | PHE195 |
| B | THR196 |
| B | PRO346 |
| B | ALA347 |
| B | HOH602 |
| B | HOH636 |
| B | HOH707 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| B | ALA336 |
| B | GLY339 |
| B | ALA341 |
| B | TRP343 |
| B | HOH650 |
| B | HOH661 |
| B | HOH747 |
| B | HOH759 |
| site_id | AC6 |
| Number of Residues | 23 |
| Details | binding site for Di-peptide PLP B 501 and GLU B 502 |
| Chain | Residue |
| A | TYR73 |
| A | ILE289 |
| B | ARG39 |
| B | GLY40 |
| B | LYS41 |
| B | SER103 |
| B | SER104 |
| B | LEU105 |
| B | TYR142 |
| B | ARG144 |
| B | VAL186 |
| B | ASN191 |
| B | ASP220 |
| B | ALA222 |
| B | TYR223 |
| B | SER256 |
| B | SER258 |
| B | LYS259 |
| B | ARG394 |
| B | HOH601 |
| B | HOH625 |
| B | HOH682 |
| B | HOH779 |
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 |
