4DAA
CRYSTALLOGRAPHIC STRUCTURE OF D-AMINO ACID AMINOTRANSFERASE IN PYRIDOXAL-5'-PHOSPHATE (PLP) FORM
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 | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 287 |
Chain | Residue |
A | TYR31 |
A | LYS145 |
A | SER180 |
A | PLP285 |
A | HOH619 |
B | ARG98 |
B | HIS100 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 287 |
Chain | Residue |
A | ARG98 |
A | HIS100 |
B | TYR31 |
B | LYS145 |
B | SER180 |
B | PLP285 |
site_id | AC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE PLP A 285 |
Chain | Residue |
A | HIS47 |
A | ARG50 |
A | ARG138 |
A | LYS145 |
A | GLU177 |
A | SER181 |
A | ASN182 |
A | LEU201 |
A | GLY203 |
A | ILE204 |
A | THR205 |
A | THR241 |
A | SO4287 |
A | HOH619 |
A | HOH629 |
site_id | AC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PLP B 285 |
Chain | Residue |
B | HIS47 |
B | ARG50 |
B | LYS145 |
B | GLU177 |
B | SER181 |
B | ASN182 |
B | LEU201 |
B | GLY203 |
B | ILE204 |
B | THR205 |
B | SER240 |
B | THR241 |
B | SO4287 |
B | HOH676 |
site_id | ASA |
Number of Residues | 6 |
Details | ACTIVE SITE A. |
Chain | Residue |
A | PLP285 |
A | LYS145 |
A | TYR31 |
B | HIS100 |
B | ARG98 |
A | GLU177 |
site_id | ASB |
Number of Residues | 6 |
Details | ESSENTIALLY THE SAME AS ASA. |
Chain | Residue |
A | HIS100 |
A | ARG98 |
B | GLU177 |
B | PLP285 |
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 |