6A2F
Crystal structure of biosynthetic alanine racemase from Pseudomonas aeruginosa
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 | 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 | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue MLI A 401 |
Chain | Residue |
A | LYS123 |
A | ARG130 |
A | LEU131 |
A | HOH514 |
B | MET304 |
B | DLY501 |
site_id | AC2 |
Number of Residues | 13 |
Details | binding site for residue DLY A 402 |
Chain | Residue |
A | MET302 |
A | ASP303 |
A | MET304 |
A | ACT403 |
B | LLP34 |
B | ARG130 |
B | TYR342 |
B | MLI503 |
B | HOH639 |
B | HOH646 |
A | TYR254 |
A | TYR273 |
A | SER301 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue ACT A 403 |
Chain | Residue |
A | TYR254 |
A | ARG279 |
A | ARG299 |
A | DLY402 |
B | LEU340 |
site_id | AC4 |
Number of Residues | 12 |
Details | binding site for residue DLY B 501 |
Chain | Residue |
A | LLP34 |
A | ARG130 |
A | TYR342 |
A | MLI401 |
A | HOH533 |
B | TYR254 |
B | TYR273 |
B | SER301 |
B | MET302 |
B | ASP303 |
B | MET304 |
B | ACT502 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue ACT B 502 |
Chain | Residue |
A | LEU340 |
A | TYR342 |
B | TYR254 |
B | ARG279 |
B | DLY501 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue MLI B 503 |
Chain | Residue |
A | MET304 |
A | DLY402 |
B | LYS123 |
B | MET128 |
B | ARG130 |
B | LEU131 |
B | HOH612 |
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 | 2 |
Details | ACT_SITE: Proton acceptor; specific for D-alanine => ECO:0000250 |
Chain | Residue | Details |
A | LLP34 | |
B | LLP34 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor; specific for L-alanine => ECO:0000250 |
Chain | Residue | Details |
A | TYR254 | |
B | TYR254 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ARG130 | |
A | MET302 | |
B | ARG130 | |
B | MET302 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
Chain | Residue | Details |
A | LLP34 | |
B | LLP34 |