1PWH
Rat Liver L-Serine Dehydratase- Complex with PYRIDOXYL-(O-METHYL-SERINE)-5-MONOPHOSPHATE
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 | 0005737 | cellular_component | cytoplasm |
| A | 0006094 | biological_process | gluconeogenesis |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006565 | biological_process | L-serine catabolic process |
| A | 0006567 | biological_process | threonine catabolic process |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0009097 | biological_process | isoleucine biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0031667 | biological_process | response to nutrient levels |
| A | 0033590 | biological_process | response to cobalamin |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0042866 | biological_process | pyruvate biosynthetic process |
| A | 0043200 | biological_process | response to amino acid |
| A | 0065003 | biological_process | protein-containing complex assembly |
| B | 0003941 | molecular_function | L-serine ammonia-lyase activity |
| B | 0004794 | molecular_function | threonine deaminase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006094 | biological_process | gluconeogenesis |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006565 | biological_process | L-serine catabolic process |
| B | 0006567 | biological_process | threonine catabolic process |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0009097 | biological_process | isoleucine biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0031667 | biological_process | response to nutrient levels |
| B | 0033590 | biological_process | response to cobalamin |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0042866 | biological_process | pyruvate biosynthetic process |
| B | 0043200 | biological_process | response to amino acid |
| B | 0065003 | biological_process | protein-containing complex assembly |
| C | 0003941 | molecular_function | L-serine ammonia-lyase activity |
| C | 0004794 | molecular_function | threonine deaminase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006094 | biological_process | gluconeogenesis |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0006565 | biological_process | L-serine catabolic process |
| C | 0006567 | biological_process | threonine catabolic process |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0009097 | biological_process | isoleucine biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0031667 | biological_process | response to nutrient levels |
| C | 0033590 | biological_process | response to cobalamin |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0042866 | biological_process | pyruvate biosynthetic process |
| C | 0043200 | biological_process | response to amino acid |
| C | 0065003 | biological_process | protein-containing complex assembly |
| D | 0003941 | molecular_function | L-serine ammonia-lyase activity |
| D | 0004794 | molecular_function | threonine deaminase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006094 | biological_process | gluconeogenesis |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0006565 | biological_process | L-serine catabolic process |
| D | 0006567 | biological_process | threonine catabolic process |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0009097 | biological_process | isoleucine biosynthetic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0031667 | biological_process | response to nutrient levels |
| D | 0033590 | biological_process | response to cobalamin |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0042866 | biological_process | pyruvate biosynthetic process |
| D | 0043200 | biological_process | response to amino acid |
| D | 0065003 | biological_process | protein-containing complex assembly |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 332 |
| Chain | Residue |
| A | VAL167 |
| A | GLY168 |
| A | GLU194 |
| A | ALA198 |
| A | SER200 |
| A | LEU223 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 333 |
| Chain | Residue |
| B | ALA198 |
| B | SER200 |
| B | LEU223 |
| B | VAL167 |
| B | GLY168 |
| B | GLU194 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K C 334 |
| Chain | Residue |
| C | VAL167 |
| C | GLY168 |
| C | GLU194 |
| C | ALA198 |
| C | SER200 |
| C | LEU223 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K D 335 |
| Chain | Residue |
| D | VAL167 |
| D | GLY168 |
| D | GLU194 |
| D | ALA198 |
| D | SER200 |
| D | LEU223 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE PLV A 328 |
| Chain | Residue |
| A | PHE40 |
| A | LYS41 |
| A | SER64 |
| A | ALA65 |
| A | ASN67 |
| A | ALA68 |
| A | PRO135 |
| A | PHE136 |
| A | SER166 |
| A | VAL167 |
| A | GLY168 |
| A | GLY169 |
| A | GLY170 |
| A | GLY171 |
| A | LEU172 |
| A | LYS221 |
| A | ALA222 |
| A | GLY224 |
| A | CYS303 |
| A | GLY304 |
| A | HOH334 |
| A | HOH350 |
| A | HOH356 |
| site_id | AC6 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE PLV B 329 |
| Chain | Residue |
| B | PHE40 |
| B | LYS41 |
| B | SER64 |
| B | ALA65 |
| B | ASN67 |
| B | ALA68 |
| B | PHE136 |
| B | SER166 |
| B | GLY168 |
| B | GLY169 |
| B | GLY170 |
| B | GLY171 |
| B | LEU172 |
| B | LYS221 |
| B | ALA222 |
| B | GLY224 |
| B | CYS303 |
| B | HOH334 |
| B | HOH336 |
| B | HOH347 |
| site_id | AC7 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE PLV C 330 |
| Chain | Residue |
| C | PHE40 |
| C | LYS41 |
| C | SER64 |
| C | ALA65 |
| C | ASN67 |
| C | ALA68 |
| C | PRO135 |
| C | PHE136 |
| C | SER166 |
| C | VAL167 |
| C | GLY168 |
| C | GLY169 |
| C | GLY170 |
| C | GLY171 |
| C | LEU172 |
| C | LYS221 |
| C | ALA222 |
| C | GLY224 |
| C | CYS303 |
| C | HOH337 |
| C | HOH339 |
| site_id | AC8 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE PLV D 331 |
| Chain | Residue |
| D | GLY170 |
| D | GLY171 |
| D | LEU172 |
| D | LYS221 |
| D | ALA222 |
| D | GLY224 |
| D | CYS303 |
| D | HOH336 |
| D | HOH339 |
| D | PHE40 |
| D | LYS41 |
| D | SER64 |
| D | ALA65 |
| D | ASN67 |
| D | ALA68 |
| D | PHE136 |
| D | SER166 |
| D | VAL167 |
| D | GLY168 |
| D | GLY169 |
Functional Information from PROSITE/UniProt
| site_id | PS00165 |
| Number of Residues | 14 |
| Details | DEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. Dssqp.SGSFKIRGI |
| Chain | Residue | Details |
| A | ASP32-ILE45 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P20132 |
| Chain | Residue | Details |
| A | VAL164 | |
| B | VAL164 | |
| C | VAL164 | |
| D | VAL164 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: N-acetylalanine => ECO:0000269|PubMed:2660911 |
| Chain | Residue | Details |
| A | ALA2 | |
| B | ALA2 | |
| C | ALA2 | |
| D | ALA2 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:14596599, ECO:0000269|PubMed:2228555, ECO:0000269|PubMed:2660911 |
| Chain | Residue | Details |
| A | LYS41 | |
| B | LYS41 | |
| C | LYS41 | |
| D | LYS41 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 14596599 |
| Chain | Residue | Details |
| A | LYS41 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 14596599 |
| Chain | Residue | Details |
| B | LYS41 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 14596599 |
| Chain | Residue | Details |
| C | LYS41 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 14596599 |
| Chain | Residue | Details |
| D | LYS41 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 186 |
| Chain | Residue | Details |
| A | LYS41 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | PHE258 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 186 |
| Chain | Residue | Details |
| B | LYS41 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | PHE258 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA3 |
| Number of Residues | 2 |
| Details | M-CSA 186 |
| Chain | Residue | Details |
| C | LYS41 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| C | PHE258 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA4 |
| Number of Residues | 2 |
| Details | M-CSA 186 |
| Chain | Residue | Details |
| D | LYS41 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| D | PHE258 | electrostatic stabiliser, hydrogen bond acceptor |
