3PQF
Crystal structure of L-lactate dehydrogenase from Bacillus subtilis mutation H171C complexed with NAD+
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 | 14 |
Details | BINDING SITE FOR RESIDUE NAD C 352 |
Chain | Residue |
C | ILE11 |
C | GLY82 |
C | ALA83 |
C | THR122 |
C | THR232 |
C | HOH332 |
C | GLY14 |
C | PHE15 |
C | VAL16 |
C | ASP37 |
C | VAL38 |
C | TYR68 |
C | CYS80 |
C | ALA81 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE NAD D 352 |
Chain | Residue |
D | GLY14 |
D | PHE15 |
D | VAL16 |
D | ASP37 |
D | VAL38 |
D | TYR68 |
D | CYS80 |
D | ALA81 |
D | GLY82 |
D | ALA83 |
D | ILE101 |
D | THR122 |
D | THR232 |
D | HOH327 |
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 | ILE175-THR181 |
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|Ref.7, ECO:0007744|PDB:3PQD |
Chain | Residue | Details |
A | HIS178 | |
B | HIS178 | |
C | HIS178 | |
D | HIS178 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|Ref.7, ECO:0007744|PDB:3PQD, ECO:0007744|PDB:3PQF |
Chain | Residue | Details |
A | PHE15 | |
B | PHE15 | |
C | PHE15 | |
D | PHE15 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|Ref.7, ECO:0007744|PDB:3PQF |
Chain | Residue | Details |
C | ASP37 | |
C | GLY82 | |
D | ASP37 | |
D | GLY82 | |
A | ASP37 | |
A | GLY82 | |
B | ASP37 | |
B | GLY82 |
site_id | SWS_FT_FI4 |
Number of Residues | 32 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488 |
Chain | Residue | Details |
A | ASN123 | |
A | SER146 | |
A | ASP151 | |
A | THR232 | |
B | LYS42 | |
B | TYR68 | |
B | GLN85 | |
B | ARG91 | |
B | ASN123 | |
B | SER146 | |
B | ASP151 | |
B | THR232 | |
C | LYS42 | |
C | TYR68 | |
C | GLN85 | |
C | ARG91 | |
C | ASN123 | |
C | SER146 | |
C | ASP151 | |
C | THR232 | |
D | LYS42 | |
D | TYR68 | |
D | GLN85 | |
D | ARG91 | |
D | ASN123 | |
D | SER146 | |
D | ASP151 | |
D | THR232 | |
A | LYS42 | |
A | TYR68 | |
A | GLN85 | |
A | ARG91 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|Ref.7, ECO:0007744|PDB:3PQD |
Chain | Residue | Details |
A | ALA121 | |
B | ALA121 | |
C | ALA121 | |
D | ALA121 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|Ref.7, ECO:0007744|PDB:3PQD |
Chain | Residue | Details |
A | ARG156 | |
B | ARG156 | |
C | ARG156 | |
D | ARG156 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|Ref.7, ECO:0007744|PDB:3PQD |
Chain | Residue | Details |
A | GLN168 | |
B | GLN168 | |
C | GLN168 | |
D | GLN168 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:17218307 |
Chain | Residue | Details |
A | TYR223 | |
B | TYR223 | |
C | TYR223 | |
D | TYR223 |