2RJH
Crystal structure of biosynthetic alaine racemase in D-cycloserine-bound form from Escherichia coli
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 | 0008360 | biological_process | regulation of cell shape |
| 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 |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0071555 | biological_process | cell wall organization |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006522 | biological_process | alanine metabolic process |
| B | 0008360 | biological_process | regulation of cell shape |
| 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 |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0071555 | biological_process | cell wall organization |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0006522 | biological_process | alanine metabolic process |
| C | 0008360 | biological_process | regulation of cell shape |
| 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 |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0071555 | biological_process | cell wall organization |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0006522 | biological_process | alanine metabolic process |
| D | 0008360 | biological_process | regulation of cell shape |
| 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 |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 360 |
| Chain | Residue |
| A | ARG19 |
| B | ARG266 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 360 |
| Chain | Residue |
| A | ARG266 |
| B | ARG19 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 360 |
| Chain | Residue |
| C | ARG19 |
| D | ARG266 |
| D | GLN315 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 361 |
| Chain | Residue |
| A | ARG162 |
| A | CYS168 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 361 |
| Chain | Residue |
| B | ARG162 |
| B | CYS168 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DCS A 362 |
| Chain | Residue |
| A | LYS34 |
| A | TYR38 |
| A | ARG129 |
| A | HIS159 |
| A | ALA193 |
| A | SER194 |
| A | ARG209 |
| A | GLY211 |
| A | ILE212 |
| A | TYR343 |
| B | TYR255 |
| B | TYR274 |
| B | ALA302 |
| B | MET303 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DCS B 362 |
| Chain | Residue |
| A | TYR255 |
| A | TYR274 |
| A | ALA302 |
| A | MET303 |
| B | LYS34 |
| B | TYR38 |
| B | ARG129 |
| B | HIS159 |
| B | ALA193 |
| B | SER194 |
| B | ARG209 |
| B | GLY211 |
| B | ILE212 |
| B | TYR343 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DCS C 362 |
| Chain | Residue |
| C | LYS34 |
| C | TYR38 |
| C | ARG129 |
| C | HIS159 |
| C | ALA193 |
| C | SER194 |
| C | ARG209 |
| C | GLY211 |
| C | ILE212 |
| C | TYR343 |
| D | TYR255 |
| D | TYR274 |
| D | ALA302 |
| D | MET303 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DCS D 360 |
| Chain | Residue |
| C | TYR255 |
| C | TYR274 |
| C | MET303 |
| D | LYS34 |
| D | TYR38 |
| D | LEU78 |
| D | ARG129 |
| D | HIS159 |
| D | ALA193 |
| D | SER194 |
| D | ARG209 |
| D | GLY211 |
| D | ILE212 |
| D | TYR343 |
Functional Information from PROSITE/UniProt
| site_id | PS00395 |
| Number of Residues | 11 |
| Details | ALANINE_RACEMASE Alanine racemase pyridoxal-phosphate attachment site. AVvKANAYGHG |
| Chain | Residue | Details |
| A | ALA31-GLY41 |
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 | TYR255 | |
| B | TYR255 | |
| C | TYR255 | |
| D | TYR255 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:18434499 |
| Chain | Residue | Details |
| A | ARG129 | |
| C | ARG129 | |
| C | MET303 | |
| D | ARG129 | |
| D | MET303 | |
| A | MET303 | |
| B | ARG129 | |
| B | MET303 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:18434499 |
| Chain | Residue | Details |
| A | LYS34 | |
| B | LYS34 | |
| C | LYS34 | |
| D | LYS34 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-carboxylysine => ECO:0000269|PubMed:18434499 |
| Chain | Residue | Details |
| A | KCX122 | |
| B | KCX122 | |
| C | KCX122 | |
| D | KCX122 |
