2RKB
Serine dehydratase like-1 from human cancer cells
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003941 | molecular_function | L-serine ammonia-lyase activity |
| A | 0004794 | molecular_function | threonine deaminase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006565 | biological_process | L-serine catabolic process |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0008881 | molecular_function | glutamate racemase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0003941 | molecular_function | L-serine ammonia-lyase activity |
| B | 0004794 | molecular_function | threonine deaminase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006565 | biological_process | L-serine catabolic process |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0008881 | molecular_function | glutamate racemase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042802 | molecular_function | identical protein binding |
| C | 0003941 | molecular_function | L-serine ammonia-lyase activity |
| C | 0004794 | molecular_function | threonine deaminase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0006565 | biological_process | L-serine catabolic process |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0008881 | molecular_function | glutamate racemase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0042802 | molecular_function | identical protein binding |
| D | 0003941 | molecular_function | L-serine ammonia-lyase activity |
| D | 0004794 | molecular_function | threonine deaminase activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0006565 | biological_process | L-serine catabolic process |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0008881 | molecular_function | glutamate racemase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0042802 | molecular_function | identical protein binding |
| E | 0003941 | molecular_function | L-serine ammonia-lyase activity |
| E | 0004794 | molecular_function | threonine deaminase activity |
| E | 0005829 | cellular_component | cytosol |
| E | 0006520 | biological_process | amino acid metabolic process |
| E | 0006565 | biological_process | L-serine catabolic process |
| E | 0006629 | biological_process | lipid metabolic process |
| E | 0008881 | molecular_function | glutamate racemase activity |
| E | 0016829 | molecular_function | lyase activity |
| E | 0016853 | molecular_function | isomerase activity |
| E | 0030170 | molecular_function | pyridoxal phosphate binding |
| E | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 401 |
| Chain | Residue |
| A | GLY174 |
| A | GLU200 |
| A | ALA204 |
| A | CYS206 |
| A | LEU229 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K B 401 |
| Chain | Residue |
| B | LEU229 |
| B | GLY174 |
| B | GLU200 |
| B | ALA204 |
| B | CYS206 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K C 401 |
| Chain | Residue |
| C | GLY174 |
| C | GLU200 |
| C | ALA204 |
| C | CYS206 |
| C | LEU229 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K D 401 |
| Chain | Residue |
| D | GLY174 |
| D | GLU200 |
| D | ALA204 |
| D | CYS206 |
| D | LEU229 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K E 401 |
| Chain | Residue |
| E | GLY174 |
| E | GLU200 |
| E | ALA204 |
| E | CYS206 |
| E | LEU229 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP A 400 |
| Chain | Residue |
| A | PHE47 |
| A | LYS48 |
| A | ASN74 |
| A | PHE142 |
| A | GLY174 |
| A | GLY175 |
| A | GLY176 |
| A | GLY177 |
| A | LEU178 |
| A | SER228 |
| A | CYS309 |
| A | HOH405 |
| A | HOH407 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP B 400 |
| Chain | Residue |
| B | PHE47 |
| B | LYS48 |
| B | ASN74 |
| B | PHE142 |
| B | GLY174 |
| B | GLY175 |
| B | GLY176 |
| B | GLY177 |
| B | LEU178 |
| B | SER228 |
| B | CYS309 |
| B | HOH405 |
| B | HOH439 |
| B | HOH463 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP C 400 |
| Chain | Residue |
| C | PHE47 |
| C | LYS48 |
| C | ASN74 |
| C | PHE142 |
| C | GLY174 |
| C | GLY175 |
| C | GLY176 |
| C | GLY177 |
| C | LEU178 |
| C | SER228 |
| C | CYS309 |
| C | HOH416 |
| C | HOH427 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PLP D 400 |
| Chain | Residue |
| D | PHE47 |
| D | LYS48 |
| D | ASN74 |
| D | PHE142 |
| D | GLY174 |
| D | GLY175 |
| D | GLY176 |
| D | GLY177 |
| D | LEU178 |
| D | SER228 |
| D | CYS309 |
| site_id | BC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP E 400 |
| Chain | Residue |
| E | PHE47 |
| E | LYS48 |
| E | ASN74 |
| E | PHE142 |
| E | GLY174 |
| E | GLY175 |
| E | GLY176 |
| E | GLY177 |
| E | LEU178 |
| E | SER228 |
| E | CYS309 |
| E | HOH466 |
| E | HOH482 |
Functional Information from PROSITE/UniProt
| site_id | PS00165 |
| Number of Residues | 14 |
| Details | DEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. Envqp.SGSFKIRGI |
| Chain | Residue | Details |
| A | GLU39-ILE52 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:18342636 |
| Chain | Residue | Details |
| A | LYS48 | |
| B | LYS48 | |
| C | LYS48 | |
| D | LYS48 | |
| E | LYS48 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1pwh |
| Chain | Residue | Details |
| A | LYS48 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1pwh |
| Chain | Residue | Details |
| B | LYS48 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1pwh |
| Chain | Residue | Details |
| C | LYS48 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1pwh |
| Chain | Residue | Details |
| D | LYS48 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1pwh |
| Chain | Residue | Details |
| E | LYS48 |
