2XXJ
Penta mutant of lactate dehydrogenase from Thermus thermophilus, ternary complex
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 |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006089 | biological_process | lactate metabolic process |
| C | 0006090 | biological_process | pyruvate metabolic process |
| C | 0006096 | biological_process | glycolytic 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 | 0005737 | cellular_component | cytoplasm |
| D | 0006089 | biological_process | lactate metabolic process |
| D | 0006090 | biological_process | pyruvate metabolic process |
| D | 0006096 | biological_process | glycolytic 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 | 10 |
| Details | BINDING SITE FOR RESIDUE OXM B 1310 |
| Chain | Residue |
| B | GLN79 |
| B | HOH2176 |
| B | ARG85 |
| B | ASN117 |
| B | LEU144 |
| B | ARG148 |
| B | HIS172 |
| B | ALA217 |
| B | THR227 |
| B | NAD1311 |
| site_id | AC2 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD B 1311 |
| Chain | Residue |
| B | GLY7 |
| B | GLY9 |
| B | MET10 |
| B | VAL11 |
| B | ASP32 |
| B | LEU33 |
| B | LEU37 |
| B | TYR62 |
| B | ALA74 |
| B | ALA75 |
| B | GLY76 |
| B | VAL77 |
| B | ALA78 |
| B | GLN79 |
| B | VAL99 |
| B | ALA115 |
| B | THR116 |
| B | ASN117 |
| B | VAL119 |
| B | SER140 |
| B | HIS172 |
| B | THR227 |
| B | ILE231 |
| B | OXM1310 |
| B | HOH2036 |
| B | HOH2063 |
| B | HOH2127 |
| B | HOH2174 |
| B | HOH2175 |
| B | HOH2176 |
| B | HOH2177 |
| B | HOH2178 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE OXM D 1311 |
| Chain | Residue |
| D | GLN79 |
| D | ARG85 |
| D | ASN117 |
| D | LEU144 |
| D | ARG148 |
| D | HIS172 |
| D | ALA217 |
| D | THR227 |
| D | NAD1312 |
| D | HOH2154 |
| site_id | AC4 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAD D 1312 |
| Chain | Residue |
| B | GLY82 |
| B | GLN87 |
| B | HOH2037 |
| B | HOH2050 |
| D | VAL6 |
| D | GLY7 |
| D | GLY9 |
| D | MET10 |
| D | VAL11 |
| D | ASP32 |
| D | LEU33 |
| D | LEU37 |
| D | TYR62 |
| D | ALA74 |
| D | ALA75 |
| D | GLY76 |
| D | VAL77 |
| D | ALA78 |
| D | GLN79 |
| D | VAL99 |
| D | ALA115 |
| D | ASN117 |
| D | SER140 |
| D | HIS172 |
| D | THR227 |
| D | ILE231 |
| D | OXM1311 |
| D | HOH2003 |
| D | HOH2120 |
| D | HOH2154 |
| D | HOH2156 |
| D | HOH2157 |
| D | HOH2158 |
| D | HOH2159 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1311 |
| Chain | Residue |
| A | ARG150 |
| A | HIS165 |
| A | TYR167 |
| A | HOH2109 |
| A | HOH2110 |
| A | HOH2138 |
| D | SER163 |
| D | HIS165 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1311 |
| Chain | Residue |
| C | HOH2141 |
| C | HOH2142 |
| C | HOH2167 |
| B | SER163 |
| B | HIS165 |
| C | ARG150 |
| C | HIS165 |
| C | TYR167 |
Functional Information from PROSITE/UniProt
| site_id | PS00064 |
| Number of Residues | 7 |
| Details | L_LDH L-lactate dehydrogenase active site. LGEHGDS |
| Chain | Residue | Details |
| A | LEU169-SER175 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|PubMed:17936781, ECO:0000305|Ref.4, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXJ |
| Chain | Residue | Details |
| A | HIS172 | |
| B | HIS172 | |
| C | HIS172 | |
| D | HIS172 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:17936781, ECO:0000269|Ref.2, ECO:0000269|Ref.4, ECO:0000305|PubMed:22319152, ECO:0007744|PDB:2E37, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXB, ECO:0007744|PDB:2XXJ, ECO:0007744|PDB:3ZZN |
| Chain | Residue | Details |
| A | MET10 | |
| D | MET10 | |
| D | ASP32 | |
| D | GLY76 | |
| A | ASP32 | |
| A | GLY76 | |
| B | MET10 | |
| B | ASP32 | |
| B | GLY76 | |
| C | MET10 | |
| C | ASP32 | |
| C | GLY76 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:17936781, ECO:0000269|Ref.4, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXB, ECO:0007744|PDB:2XXJ |
| Chain | Residue | Details |
| A | TYR62 | |
| B | TYR62 | |
| C | TYR62 | |
| D | TYR62 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|PubMed:17936781, ECO:0000305|Ref.4, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXJ |
| Chain | Residue | Details |
| A | GLN79 | |
| A | ASP145 | |
| B | GLN79 | |
| B | ASP145 | |
| C | GLN79 | |
| C | ASP145 | |
| D | GLN79 | |
| D | ASP145 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:17936781, ECO:0000305|Ref.4, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXJ |
| Chain | Residue | Details |
| A | ARG85 | |
| A | THR227 | |
| B | ARG85 | |
| B | THR227 | |
| C | ARG85 | |
| C | THR227 | |
| D | ARG85 | |
| D | THR227 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:17936781, ECO:0000269|Ref.4, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXJ |
| Chain | Residue | Details |
| A | ALA115 | |
| B | ALA115 | |
| C | ALA115 | |
| D | ALA115 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488 |
| Chain | Residue | Details |
| A | ASN117 | |
| D | ASN117 | |
| D | ARG150 | |
| D | HIS165 | |
| A | ARG150 | |
| A | HIS165 | |
| B | ASN117 | |
| B | ARG150 | |
| B | HIS165 | |
| C | ASN117 | |
| C | ARG150 | |
| C | HIS165 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17936781, ECO:0000269|Ref.4, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXJ |
| Chain | Residue | Details |
| A | SER140 | |
| B | SER140 | |
| C | SER140 | |
| D | SER140 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000255|HAMAP-Rule:MF_00488 |
| Chain | Residue | Details |
| A | TYR218 | |
| B | TYR218 | |
| C | TYR218 | |
| D | TYR218 |
