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 | Active site: {"description":"Proton acceptor; specific for D-alanine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor; specific for L-alanine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
