Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0006534 | biological_process | cysteine metabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0031071 | molecular_function | cysteine desulfurase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue PMP A 501 |
| Chain | Residue |
| A | ALA28 |
| A | LYS224 |
| A | THR275 |
| A | HOH609 |
| A | HOH669 |
| A | HOH691 |
| A | THR92 |
| A | THR93 |
| A | HIS121 |
| A | ASN173 |
| A | ASP198 |
| A | ALA200 |
| A | SER221 |
| A | HIS223 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 502 |
| Chain | Residue |
| A | HIS304 |
| A | ALA308 |
| A | GLU326 |
| A | GLU327 |
| A | ARG328 |
| A | HOH608 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 503 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | ARG75 |
| A | ASN79 |
| A | GLN211 |
| A | ARG313 |
| A | GLN316 |
| A | HOH604 |
| A | HOH755 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue PEG A 505 |
| Chain | Residue |
| A | SER300 |
| A | ARG328 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue PEG A 506 |
| Chain | Residue |
| A | THR4 |
| A | ARG7 |
| A | THR384 |
| A | GLU386 |
| A | HOH602 |
| A | HOH737 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue PEG A 507 |
| Chain | Residue |
| A | PRO11 |
| A | GLN15 |
| A | ASN46 |
| A | GLN47 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue PEG A 508 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue PEG A 509 |
| Chain | Residue |
| A | VAL347 |
| A | GLU351 |
| A | LYS397 |
| A | TYR401 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 510 |
| Chain | Residue |
| A | LYS43 |
| A | GLN47 |
| A | TYR48 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue PEG A 511 |
| Chain | Residue |
| A | ASP5 |
| A | GLN9 |
| A | PHE290 |
| A | GLU293 |
| A | HOH603 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue PG4 A 512 |
| Chain | Residue |
| A | HIS53 |
| A | GLU252 |
| A | LYS265 |
| A | TRP269 |
| A | HOH714 |
Functional Information from PROSITE/UniProt
| site_id | PS00595 |
| Number of Residues | 20 |
| Details | AA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. CDFFalSSHKmcgpt.GvGvL |
| Chain | Residue | Details |
| A | CYS215-LEU234 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Cysteine persulfide intermediate","evidences":[{"source":"PubMed","id":"27382962","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31587510","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"31587510","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5J8Q","evidenceCode":"ECO:0007744"}]} |
