3DAA
CRYSTALLOGRAPHIC STRUCTURE OF D-AMINO ACID AMINOTRANSFERASE INACTIVATED BY PYRIDOXYL-D-ALANINE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019478 | biological_process | D-amino acid catabolic process |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0046394 | biological_process | carboxylic acid biosynthetic process |
| A | 0046416 | biological_process | D-amino acid metabolic process |
| A | 0046437 | biological_process | D-amino acid biosynthetic process |
| A | 0047810 | molecular_function | D-alanine-2-oxoglutarate aminotransferase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019478 | biological_process | D-amino acid catabolic process |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0046394 | biological_process | carboxylic acid biosynthetic process |
| B | 0046416 | biological_process | D-amino acid metabolic process |
| B | 0046437 | biological_process | D-amino acid biosynthetic process |
| B | 0047810 | molecular_function | D-alanine-2-oxoglutarate aminotransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PDD A 285 |
| Chain | Residue |
| A | TYR31 |
| A | ARG50 |
| A | LYS145 |
| A | GLU177 |
| A | GLY178 |
| A | SER180 |
| A | SER181 |
| A | ASN182 |
| A | GLY203 |
| A | ILE204 |
| A | THR205 |
| A | SER240 |
| A | THR241 |
| A | HOH675 |
| A | HOH692 |
| A | HOH718 |
| B | ARG98 |
| B | HIS100 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE PDD B 285 |
| Chain | Residue |
| A | ARG98 |
| A | HIS100 |
| B | TYR31 |
| B | HIS47 |
| B | ARG50 |
| B | LYS145 |
| B | GLU177 |
| B | SER180 |
| B | SER181 |
| B | ASN182 |
| B | LEU201 |
| B | GLY203 |
| B | ILE204 |
| B | THR205 |
| B | SER240 |
| B | THR241 |
| B | HOH686 |
| B | HOH697 |
| B | HOH804 |
| site_id | ASA |
| Number of Residues | 6 |
| Details | ACTIVE SITE A, INACTIVATED BY PHOSPHOPYRIDOXYL D-ALANINE. |
| Chain | Residue |
| A | PDD285 |
| A | LYS145 |
| A | TYR31 |
| B | HIS100 |
| B | ARG98 |
| A | GLU177 |
| site_id | ASB |
| Number of Residues | 6 |
| Details | ACTIVE SITE B, INACTIVATED BY PHOSPHOPYRIDOXYL D-ALANINE. |
| Chain | Residue |
| A | HIS100 |
| A | ARG98 |
| B | GLU177 |
| B | PDD285 |
| B | LYS145 |
| B | TYR31 |
Functional Information from PROSITE/UniProt
| site_id | PS00770 |
| Number of Residues | 30 |
| Details | AA_TRANSFER_CLASS_4 Aminotransferases class-IV signature. EgSssNVFgikdgi......LyThpannmi.LkGItR |
| Chain | Residue | Details |
| A | GLU177-ARG206 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"7626635","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9538014","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"7626635","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1daa |
| Chain | Residue | Details |
| A | LEU201 | |
| A | LYS145 | |
| A | GLU177 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1daa |
| Chain | Residue | Details |
| B | LEU201 | |
| B | LYS145 | |
| B | GLU177 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1daa |
| Chain | Residue | Details |
| A | ILE144 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1daa |
| Chain | Residue | Details |
| B | ILE144 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 66 |
| Chain | Residue | Details |
| A | TYR31 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| A | LYS145 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | GLU177 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| A | LEU201 | steric role, van der waals interaction |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 66 |
| Chain | Residue | Details |
| B | TYR31 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| B | LYS145 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | GLU177 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| B | LEU201 | steric role, van der waals interaction |
