2DY3
Crystal Structure of alanine racemase from Corynebacterium glutamicum
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 |
D | 0003824 | molecular_function | catalytic activity |
D | 0005829 | cellular_component | cytosol |
D | 0006522 | biological_process | alanine metabolic process |
D | 0008784 | molecular_function | alanine racemase activity |
D | 0009252 | biological_process | peptidoglycan biosynthetic process |
D | 0016853 | molecular_function | isomerase activity |
D | 0030170 | molecular_function | pyridoxal phosphate binding |
D | 0030632 | biological_process | D-alanine biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PLP A 401 |
Chain | Residue |
A | VAL32 |
A | LEU217 |
A | TYR346 |
B | ASP305 |
B | HOH567 |
A | LYS34 |
A | TYR38 |
A | TRP80 |
A | HIS158 |
A | ASN198 |
A | SER199 |
A | ARG214 |
A | GLY216 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PLP B 401 |
Chain | Residue |
A | HOH556 |
B | VAL32 |
B | LYS34 |
B | TYR38 |
B | TRP80 |
B | HIS158 |
B | ASN198 |
B | SER199 |
B | ARG214 |
B | PRO215 |
B | GLY216 |
B | LEU217 |
B | TYR346 |
site_id | AC3 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PLP C 401 |
Chain | Residue |
C | VAL32 |
C | LYS34 |
C | TYR38 |
C | TRP80 |
C | HIS158 |
C | ASN198 |
C | SER199 |
C | PRO200 |
C | ARG214 |
C | PRO215 |
C | GLY216 |
C | LEU217 |
C | TYR346 |
C | HOH535 |
site_id | AC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PLP D 401 |
Chain | Residue |
C | HOH536 |
D | VAL32 |
D | LYS34 |
D | TYR38 |
D | TRP80 |
D | HIS158 |
D | ASN198 |
D | SER199 |
D | ARG214 |
D | PRO215 |
D | GLY216 |
D | LEU217 |
D | TYR346 |
D | HOH463 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor; specific for D-alanine => ECO:0000255|HAMAP-Rule:MF_01201 |
Chain | Residue | Details |
A | LYS34 | |
B | LYS34 | |
C | LYS34 | |
D | LYS34 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor; specific for L-alanine => ECO:0000255|HAMAP-Rule:MF_01201 |
Chain | Residue | Details |
A | TYR256 | |
B | TYR256 | |
C | TYR256 | |
D | TYR256 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01201 |
Chain | Residue | Details |
A | ARG129 | |
A | MET304 | |
B | ARG129 | |
B | MET304 | |
C | ARG129 | |
C | MET304 | |
D | ARG129 | |
D | MET304 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
Chain | Residue | Details |
A | LYS34 | |
B | LYS34 | |
C | LYS34 | |
D | LYS34 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1bd0 |
Chain | Residue | Details |
A | CYS303 | |
B | LYS34 | |
B | ARG129 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1bd0 |
Chain | Residue | Details |
A | LYS34 | |
A | ARG129 | |
B | CYS303 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1bd0 |
Chain | Residue | Details |
C | CYS303 | |
D | LYS34 | |
D | ARG129 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1bd0 |
Chain | Residue | Details |
D | CYS303 | |
C | LYS34 | |
C | ARG129 |