3H3J
Crystal structure of lactate dehydrogenase mutant (A85R) from staphylococcus aureus complexed with NAD and pyruvate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006089 | biological_process | lactate metabolic process |
| A | 0006090 | biological_process | pyruvate metabolic process |
| A | 0006096 | biological_process | glycolytic 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 | 0005737 | cellular_component | cytoplasm |
| B | 0006089 | biological_process | lactate metabolic process |
| B | 0006090 | biological_process | pyruvate metabolic process |
| B | 0006096 | biological_process | glycolytic 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD A 500 |
| Chain | Residue |
| A | GLY15 |
| A | ARG85 |
| A | ALA122 |
| A | THR123 |
| A | ASN124 |
| A | SER147 |
| A | LEU151 |
| A | HIS179 |
| A | THR232 |
| A | VAL236 |
| A | HOH327 |
| A | ALA16 |
| A | HOH349 |
| A | HOH394 |
| A | HOH399 |
| A | HOH416 |
| A | HOH434 |
| A | HOH447 |
| A | HOH453 |
| A | HOH464 |
| A | PYR501 |
| A | VAL17 |
| A | ASP38 |
| A | LEU39 |
| A | CYS81 |
| A | ALA82 |
| A | GLY83 |
| A | ALA84 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PYR A 501 |
| Chain | Residue |
| A | GLN86 |
| A | ARG92 |
| A | ASN124 |
| A | LEU151 |
| A | ARG155 |
| A | HIS179 |
| A | ALA222 |
| A | THR232 |
| A | NAD500 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 502 |
| Chain | Residue |
| A | SER188 |
| A | HIS189 |
| A | HOH344 |
| B | HIS189 |
| B | HOH349 |
| site_id | AC4 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD B 500 |
| Chain | Residue |
| B | GLY15 |
| B | ALA16 |
| B | VAL17 |
| B | ASP38 |
| B | LEU39 |
| B | CYS81 |
| B | ALA82 |
| B | GLY83 |
| B | ALA84 |
| B | ARG85 |
| B | ILE102 |
| B | ALA122 |
| B | THR123 |
| B | ASN124 |
| B | SER147 |
| B | LEU151 |
| B | HIS179 |
| B | THR232 |
| B | VAL236 |
| B | HOH327 |
| B | HOH348 |
| B | HOH371 |
| B | HOH406 |
| B | HOH421 |
| B | HOH423 |
| B | HOH424 |
| B | HOH437 |
| B | PYR501 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PYR B 501 |
| Chain | Residue |
| B | GLN86 |
| B | ARG92 |
| B | ASN124 |
| B | LEU151 |
| B | ARG155 |
| B | HIS179 |
| B | ALA222 |
| B | THR232 |
| B | NAD500 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 502 |
| Chain | Residue |
| A | ARG284 |
| A | ASN285 |
| B | PHE164 |
| B | VAL166 |
| B | GLN195 |
Functional Information from PROSITE/UniProt
| site_id | PS00064 |
| Number of Residues | 7 |
| Details | L_LDH L-lactate dehydrogenase active site. IGEHGDT |
| Chain | Residue | Details |
| A | ILE176-THR182 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|Ref.3, ECO:0000305|Ref.4, ECO:0007744|PDB:3D4P, ECO:0007744|PDB:3H3J |
| Chain | Residue | Details |
| A | HIS179 | |
| B | HIS179 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|Ref.3, ECO:0000269|Ref.4, ECO:0007744|PDB:3D4P, ECO:0007744|PDB:3H3J |
| Chain | Residue | Details |
| A | ALA16 | |
| B | ALA16 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|Ref.3, ECO:0000269|Ref.4, ECO:0007744|PDB:3D4P, ECO:0007744|PDB:3H3J |
| Chain | Residue | Details |
| A | THR232 | |
| B | ASP38 | |
| B | GLY83 | |
| B | THR232 | |
| A | ASP38 | |
| A | GLY83 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488 |
| Chain | Residue | Details |
| A | GLN86 | |
| A | SER105 | |
| A | ASN124 | |
| B | LYS43 | |
| B | TYR69 | |
| B | GLN86 | |
| B | SER105 | |
| B | ASN124 | |
| A | LYS43 | |
| A | TYR69 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|Ref.4, ECO:0007744|PDB:3H3J |
| Chain | Residue | Details |
| B | ARG92 | |
| B | SER147 | |
| A | ARG92 | |
| A | SER147 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|Ref.4, ECO:0007744|PDB:3H3J |
| Chain | Residue | Details |
| A | ALA122 | |
| B | ALA122 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|Ref.3, ECO:0000305|Ref.4, ECO:0007744|PDB:3D4P, ECO:0007744|PDB:3H3J |
| Chain | Residue | Details |
| A | ASP152 | |
| B | ASP152 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000255|HAMAP-Rule:MF_00488 |
| Chain | Residue | Details |
| A | TYR223 | |
| B | TYR223 |
