2DAA
CRYSTALLOGRAPHIC STRUCTURE OF D-AMINO ACID AMINOTRANSFERASE INACTIVATED BY D-CYCLOSERINE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0008483 | molecular_function | transaminase 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 | 0008483 | molecular_function | transaminase 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 | 20 |
| Details | BINDING SITE FOR RESIDUE DCS A 285 |
| Chain | Residue |
| A | TYR31 |
| A | VAL33 |
| A | ARG50 |
| A | LYS145 |
| A | GLU177 |
| A | SER180 |
| A | SER181 |
| A | ASN182 |
| A | LEU201 |
| A | GLY203 |
| A | ILE204 |
| A | THR205 |
| A | SER240 |
| A | THR241 |
| A | HOH610 |
| A | HOH709 |
| A | HOH712 |
| A | HOH713 |
| B | ARG98 |
| B | HIS100 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE DCS B 285 |
| Chain | Residue |
| A | ARG98 |
| A | HIS100 |
| B | TYR31 |
| B | VAL33 |
| 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 | HOH626 |
| B | HOH652 |
| B | HOH708 |
| B | HOH717 |
| site_id | ASA |
| Number of Residues | 6 |
| Details | ACTIVE SITE CONTAINING PLP COFACTOR BLOCKED WITH CYCLOSERINE. TWO WATER MOLECULES ARE ALSO TIGHTLY ASSOCIATED WITH THE SITE. |
| Chain | Residue |
| A | DCS285 |
| A | LYS145 |
| A | TYR31 |
| B | HIS100 |
| B | ARG98 |
| A | GLU177 |
| site_id | ASB |
| Number of Residues | 6 |
| Details | ESSENTIALLY IDENTICAL TO ASA. |
| Chain | Residue |
| A | HIS100 |
| A | ARG98 |
| B | GLU177 |
| B | DCS285 |
| 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 | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:7626635 |
| Chain | Residue | Details |
| A | SER146 | |
| B | SER146 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:9538014 |
| Chain | Residue | Details |
| A | GLU32 | |
| B | GLY178 | |
| A | LEU51 | |
| A | ALA99 | |
| A | GLN101 | |
| A | GLY178 | |
| B | GLU32 | |
| B | LEU51 | |
| B | ALA99 | |
| B | GLN101 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:7626635 |
| Chain | Residue | Details |
| A | SER146 | |
| B | SER146 |
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 | GLU32 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| A | SER146 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | GLY178 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| A | LYS202 | steric role, van der waals interaction |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 66 |
| Chain | Residue | Details |
| B | GLU32 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| B | SER146 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | GLY178 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| B | LYS202 | steric role, van der waals interaction |
