1D2F
X-RAY STRUCTURE OF MALY FROM ESCHERICHIA COLI: A PYRIDOXAL-5'-PHOSPHATE-DEPENDENT ENZYME ACTING AS A MODULATOR IN MAL GENE EXPRESSION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0006351 | biological_process | DNA-templated transcription |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009086 | biological_process | obsolete methionine biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0047804 | molecular_function | cysteine-S-conjugate beta-lyase activity |
| A | 0080146 | molecular_function | L-cysteine desulfhydrase activity |
| A | 0140297 | molecular_function | DNA-binding transcription factor binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0006351 | biological_process | DNA-templated transcription |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0009086 | biological_process | obsolete methionine biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0047804 | molecular_function | cysteine-S-conjugate beta-lyase activity |
| B | 0080146 | molecular_function | L-cysteine desulfhydrase activity |
| B | 0140297 | molecular_function | DNA-binding transcription factor binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP A 400 |
| Chain | Residue |
| A | SER95 |
| A | HOH427 |
| A | HOH430 |
| B | TYR61 |
| A | VAL96 |
| A | ILE97 |
| A | CYS169 |
| A | ASN173 |
| A | ASP201 |
| A | ILE203 |
| A | HIS204 |
| A | LYS233 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PLP B 400 |
| Chain | Residue |
| A | TYR61 |
| B | SER95 |
| B | VAL96 |
| B | ILE97 |
| B | CYS169 |
| B | ASN173 |
| B | ASP201 |
| B | ILE203 |
| B | HIS204 |
| B | LYS233 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"10698925","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7665481","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TYR121 | |
| A | ASP201 | |
| B | GLY60 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | GLY60 | |
| B | TYR121 | |
| B | ASP201 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TYR121 | |
| A | ASP201 | |
| A | LYS233 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | TYR121 | |
| B | ASP201 | |
| B | LYS233 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | HIS204 | |
| A | PHE235 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | HIS204 | |
| B | PHE235 |
