2LDB
STRUCTURE DETERMINATION AND REFINEMENT OF BACILLUS STEAROTHERMOPHILUS LACTATE DEHYDROGENASE
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 |
A | 0051287 | molecular_function | NAD binding |
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 |
B | 0051287 | molecular_function | NAD binding |
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 |
C | 0051287 | molecular_function | NAD binding |
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 |
D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | FBA |
Number of Residues | 10 |
Details | FBP binding site |
Chain | Residue |
A | ARG171 |
A | PRO182 |
A | GLN183 |
A | ASN184 |
A | VAL185 |
A | HIS186 |
A | ALA187 |
A | TYR188 |
A | GLY207 |
A | ILE269 |
site_id | FBB |
Number of Residues | 10 |
Details | FBP binding site |
Chain | Residue |
B | ARG171 |
B | PRO182 |
B | GLN183 |
B | ASN184 |
B | VAL185 |
B | HIS186 |
B | ALA187 |
B | TYR188 |
B | GLY207 |
B | ILE269 |
site_id | FBC |
Number of Residues | 10 |
Details | FBP binding site |
Chain | Residue |
C | VAL185 |
C | HIS186 |
C | ALA187 |
C | TYR188 |
C | GLY207 |
C | ILE269 |
C | ARG171 |
C | PRO182 |
C | GLN183 |
C | ASN184 |
site_id | FBD |
Number of Residues | 10 |
Details | FBP binding site |
Chain | Residue |
D | ARG171 |
D | PRO182 |
D | GLN183 |
D | ASN184 |
D | VAL185 |
D | HIS186 |
D | ALA187 |
D | TYR188 |
D | GLY207 |
D | ILE269 |
site_id | NAA |
Number of Residues | 25 |
Details | NAD binding site |
Chain | Residue |
A | ILE26 |
A | ALA53 |
A | ASN54 |
A | LYS57 |
A | TYR83 |
A | CYS95 |
A | ALA96 |
A | GLY97 |
A | ALA98 |
A | ILE116 |
A | ILE120 |
A | GLY27 |
A | ALA136 |
A | THR137 |
A | ASN138 |
A | SER161 |
A | LEU165 |
A | HIS193 |
A | ALA28 |
A | GLY29 |
A | PHE30 |
A | VAL31 |
A | GLY32 |
A | ILE51 |
A | ASP52 |
site_id | NAB |
Number of Residues | 25 |
Details | NAD binding site |
Chain | Residue |
B | ILE26 |
B | GLY27 |
B | ALA28 |
B | GLY29 |
B | PHE30 |
B | VAL31 |
B | GLY32 |
B | ILE51 |
B | ASP52 |
B | ALA53 |
B | ASN54 |
B | LYS57 |
B | TYR83 |
B | CYS95 |
B | ALA96 |
B | GLY97 |
B | ALA98 |
B | ILE116 |
B | ILE120 |
B | ALA136 |
B | THR137 |
B | ASN138 |
B | SER161 |
B | LEU165 |
B | HIS193 |
site_id | NAC |
Number of Residues | 25 |
Details | NAD binding site |
Chain | Residue |
C | ILE26 |
C | GLY27 |
C | ALA28 |
C | GLY29 |
C | PHE30 |
C | VAL31 |
C | GLY32 |
C | ILE51 |
C | ASP52 |
C | ALA53 |
C | ASN54 |
C | LYS57 |
C | TYR83 |
C | CYS95 |
C | ALA96 |
C | GLY97 |
C | ALA98 |
C | ILE116 |
C | ILE120 |
C | ALA136 |
C | THR137 |
C | ASN138 |
C | SER161 |
C | LEU165 |
C | HIS193 |
site_id | NAD |
Number of Residues | 25 |
Details | NAD binding site |
Chain | Residue |
D | ILE26 |
D | GLY27 |
D | ALA28 |
D | GLY29 |
D | PHE30 |
D | VAL31 |
D | GLY32 |
D | ILE51 |
D | ASP52 |
D | ALA53 |
D | ASN54 |
D | LYS57 |
D | TYR83 |
D | CYS95 |
D | ALA96 |
D | GLY97 |
D | ALA98 |
D | ILE116 |
D | ILE120 |
D | ALA136 |
D | THR137 |
D | ASN138 |
D | SER161 |
D | LEU165 |
D | HIS193 |
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 | ILE190-THR196 |
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:1731077, ECO:0007744|PDB:1LDN |
Chain | Residue | Details |
A | HIS193 | |
B | HIS193 | |
C | HIS193 | |
D | HIS193 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:1731077, ECO:0000269|PubMed:2330370, ECO:0007744|PDB:1LDN, ECO:0007744|PDB:2LDB |
Chain | Residue | Details |
A | PHE30 | |
D | PHE30 | |
D | ASP52 | |
D | ALA136 | |
A | ASP52 | |
A | ALA136 | |
B | PHE30 | |
B | ASP52 | |
B | ALA136 | |
C | PHE30 | |
C | ASP52 | |
C | ALA136 |
site_id | SWS_FT_FI3 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488 |
Chain | Residue | Details |
A | LYS57 | |
B | GLN100 | |
B | SER119 | |
B | ASN138 | |
C | LYS57 | |
C | TYR83 | |
C | GLY97 | |
C | GLN100 | |
C | SER119 | |
C | ASN138 | |
D | LYS57 | |
A | TYR83 | |
D | TYR83 | |
D | GLY97 | |
D | GLN100 | |
D | SER119 | |
D | ASN138 | |
A | GLY97 | |
A | GLN100 | |
A | SER119 | |
A | ASN138 | |
B | LYS57 | |
B | TYR83 | |
B | GLY97 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|PubMed:1731077, ECO:0007744|PDB:1LDN |
Chain | Residue | Details |
A | ARG106 | |
D | ARG106 | |
D | ASP166 | |
D | THR247 | |
A | ASP166 | |
A | THR247 | |
B | ARG106 | |
B | ASP166 | |
B | THR247 | |
C | ARG106 | |
C | ASP166 | |
C | THR247 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:1731077, ECO:0000269|PubMed:2330370, ECO:0007744|PDB:1LDN, ECO:0007744|PDB:2LDB |
Chain | Residue | Details |
A | SER161 | |
A | GLN183 | |
B | SER161 | |
B | GLN183 | |
C | SER161 | |
C | GLN183 | |
D | SER161 | |
D | GLN183 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:2330370, ECO:0007744|PDB:2LDB |
Chain | Residue | Details |
A | ARG171 | |
B | ARG171 | |
C | ARG171 | |
D | ARG171 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine => ECO:0000255|HAMAP-Rule:MF_00488 |
Chain | Residue | Details |
A | TYR238 | |
B | TYR238 | |
C | TYR238 | |
D | TYR238 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
A | ASP166 | |
A | HIS193 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
B | ASP166 | |
B | HIS193 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
C | ASP166 | |
C | HIS193 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
D | ASP166 | |
D | HIS193 |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
A | HIS193 | |
A | ASP166 | |
A | ARG169 |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
B | HIS193 | |
B | ASP166 | |
B | ARG169 |
site_id | CSA7 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
C | HIS193 | |
C | ASP166 | |
C | ARG169 |
site_id | CSA8 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
D | HIS193 | |
D | ASP166 | |
D | ARG169 |