1HYH
CRYSTAL STRUCTURE OF L-2-HYDROXYISOCAPROATE DEHYDROGENASE FROM LACTOBACILLUS CONFUSUS AT 2.2 ANGSTROMS RESOLUTION-AN EXAMPLE OF STRONG ASYMMETRY BETWEEN SUBUNITS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| A | 0006089 | biological_process | lactate metabolic process |
| A | 0006090 | biological_process | pyruvate metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| B | 0006089 | biological_process | lactate metabolic process |
| B | 0006090 | biological_process | pyruvate metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| C | 0006089 | biological_process | lactate metabolic process |
| C | 0006090 | biological_process | pyruvate metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0019752 | biological_process | carboxylic acid metabolic process |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| D | 0006089 | biological_process | lactate metabolic process |
| D | 0006090 | biological_process | pyruvate metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0019752 | biological_process | carboxylic acid metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 331 |
| Chain | Residue |
| A | ASN143 |
| A | LEU170 |
| A | ARG174 |
| A | HIS198 |
| A | THR248 |
| A | NAD330 |
| A | HOH403 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 331 |
| Chain | Residue |
| B | ARG174 |
| B | HIS198 |
| B | THR248 |
| B | NAD330 |
| B | ASN143 |
| B | LEU170 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 331 |
| Chain | Residue |
| C | ARG174 |
| C | HIS198 |
| C | THR248 |
| C | NAD330 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D 331 |
| Chain | Residue |
| D | LEU170 |
| D | ARG174 |
| D | HIS198 |
| D | THR248 |
| D | NAD330 |
| site_id | AC5 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD A 330 |
| Chain | Residue |
| A | GLY28 |
| A | GLY30 |
| A | ASN31 |
| A | VAL32 |
| A | ASP53 |
| A | ALA54 |
| A | THR96 |
| A | LEU97 |
| A | GLY98 |
| A | ASN99 |
| A | ILE100 |
| A | GLU114 |
| A | MET121 |
| A | ILE141 |
| A | SER142 |
| A | ASN143 |
| A | THR166 |
| A | LEU170 |
| A | HIS198 |
| A | THR248 |
| A | VAL252 |
| A | SO4331 |
| A | HOH339 |
| A | HOH367 |
| A | HOH388 |
| A | HOH389 |
| A | HOH397 |
| A | HOH400 |
| A | HOH410 |
| site_id | AC6 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD B 330 |
| Chain | Residue |
| B | LEU29 |
| B | GLY30 |
| B | ASN31 |
| B | VAL32 |
| B | ASP53 |
| B | ALA54 |
| B | THR96 |
| B | LEU97 |
| B | GLY98 |
| B | ASN99 |
| B | ILE100 |
| B | GLU114 |
| B | MET121 |
| B | ILE141 |
| B | SER142 |
| B | ASN143 |
| B | VAL145 |
| B | LEU170 |
| B | HIS198 |
| B | THR248 |
| B | VAL252 |
| B | SO4331 |
| B | HOH342 |
| B | HOH370 |
| B | HOH390 |
| B | HOH391 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAD C 330 |
| Chain | Residue |
| C | GLY28 |
| C | GLY30 |
| C | ASN31 |
| C | VAL32 |
| C | ASP53 |
| C | ALA54 |
| C | THR96 |
| C | LEU97 |
| C | GLY98 |
| C | MET121 |
| C | ILE141 |
| C | SER142 |
| C | ASN143 |
| C | LEU170 |
| C | HIS198 |
| C | THR248 |
| C | SO4331 |
| C | HOH341 |
| C | HOH366 |
| C | HOH397 |
| C | HOH404 |
| D | HOH399 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NAD D 330 |
| Chain | Residue |
| C | HOH396 |
| D | GLY28 |
| D | LEU29 |
| D | GLY30 |
| D | ASN31 |
| D | VAL32 |
| D | ASP53 |
| D | ALA54 |
| D | THR96 |
| D | LEU97 |
| D | GLY98 |
| D | MET121 |
| D | SER142 |
| D | ASN143 |
| D | LEU170 |
| D | HIS198 |
| D | THR248 |
| D | VAL252 |
| D | SO4331 |
| D | HOH348 |
| D | HOH372 |
Functional Information from PROSITE/UniProt
| site_id | PS00064 |
| Number of Residues | 7 |
| Details | L_LDH L-lactate dehydrogenase active site. LGEHGNS |
| Chain | Residue | Details |
| A | LEU195-SER201 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10002 |
| Chain | Residue | Details |
| A | GLY199 | |
| B | GLY199 | |
| C | GLY199 | |
| D | GLY199 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:7643402 |
| Chain | Residue | Details |
| A | ALA54 | |
| B | ALA54 | |
| C | ALA54 | |
| D | ALA54 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | PHE112 | |
| D | PHE112 | |
| D | PRO144 | |
| D | MET175 | |
| A | PRO144 | |
| A | MET175 | |
| B | PHE112 | |
| B | PRO144 | |
| B | MET175 | |
| C | PHE112 | |
| C | PRO144 | |
| C | MET175 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | HIS198 | |
| A | ASP171 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | HIS198 | |
| B | ASP171 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| C | HIS198 | |
| C | ASP171 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| D | HIS198 | |
| D | ASP171 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | HIS198 | |
| A | ARG174 | |
| A | ASP171 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | HIS198 | |
| B | ARG174 | |
| B | ASP171 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| C | HIS198 | |
| C | ARG174 | |
| C | ASP171 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| D | HIS198 | |
| D | ARG174 | |
| D | ASP171 |
