3E6E
Crystal structure of Alanine racemase from E.faecalis complex with cycloserine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0005829 | cellular_component | cytosol |
A | 0006522 | biological_process | alanine metabolic process |
A | 0008784 | molecular_function | alanine racemase activity |
A | 0009252 | biological_process | peptidoglycan biosynthetic process |
A | 0016853 | molecular_function | isomerase activity |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0030632 | biological_process | D-alanine biosynthetic process |
B | 0003824 | molecular_function | catalytic activity |
B | 0005829 | cellular_component | cytosol |
B | 0006522 | biological_process | alanine metabolic process |
B | 0008784 | molecular_function | alanine racemase activity |
B | 0009252 | biological_process | peptidoglycan biosynthetic process |
B | 0016853 | molecular_function | isomerase activity |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0030632 | biological_process | D-alanine biosynthetic process |
C | 0003824 | molecular_function | catalytic activity |
C | 0005829 | cellular_component | cytosol |
C | 0006522 | biological_process | alanine metabolic process |
C | 0008784 | molecular_function | alanine racemase activity |
C | 0009252 | biological_process | peptidoglycan biosynthetic process |
C | 0016853 | molecular_function | isomerase activity |
C | 0030170 | molecular_function | pyridoxal phosphate binding |
C | 0030632 | biological_process | D-alanine biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE DCS A 372 |
Chain | Residue |
A | VAL38 |
A | VAL225 |
A | TYR356 |
A | HOH374 |
C | TYR267 |
C | TYR286 |
C | CYS313 |
C | MET314 |
A | LYS40 |
A | TYR44 |
A | LEU86 |
A | ARG139 |
A | HIS169 |
A | SER207 |
A | ARG222 |
A | GLY224 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE DCS B 372 |
Chain | Residue |
B | VAL38 |
B | LYS40 |
B | TYR44 |
B | ARG139 |
B | HIS169 |
B | SER207 |
B | ARG222 |
B | GLY224 |
B | VAL225 |
B | TYR267 |
B | TYR286 |
B | MET314 |
B | TYR356 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE DCS C 372 |
Chain | Residue |
A | TYR267 |
A | TYR286 |
A | CYS313 |
A | MET314 |
C | LYS40 |
C | TYR44 |
C | LEU86 |
C | ARG139 |
C | HIS169 |
C | ASN206 |
C | SER207 |
C | ARG222 |
C | GLY224 |
C | VAL225 |
C | TYR356 |
C | HOH374 |
Functional Information from PROSITE/UniProt
site_id | PS00395 |
Number of Residues | 11 |
Details | ALANINE_RACEMASE Alanine racemase pyridoxal-phosphate attachment site. AVvKANGYGHG |
Chain | Residue | Details |
A | ALA37-GLY47 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1bd0 |
Chain | Residue | Details |
A | LYS40 | |
A | ARG139 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1bd0 |
Chain | Residue | Details |
B | LYS40 | |
B | ARG139 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1bd0 |
Chain | Residue | Details |
C | LYS40 | |
C | ARG139 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1bd0 |
Chain | Residue | Details |
A | CYS313 | |
A | TYR267 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1bd0 |
Chain | Residue | Details |
B | CYS313 | |
B | TYR267 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1bd0 |
Chain | Residue | Details |
C | CYS313 | |
C | TYR267 |