1T2F
Human B lactate dehydrogenase complexed with NAD+ and 4-hydroxy-1,2,5-oxadiazole-3-carboxylic acid
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004457 | molecular_function | lactate dehydrogenase activity |
A | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005743 | cellular_component | mitochondrial inner membrane |
A | 0005829 | cellular_component | cytosol |
A | 0006089 | biological_process | lactate metabolic process |
A | 0016020 | cellular_component | membrane |
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 | 0019674 | biological_process | NAD+ metabolic process |
A | 0019752 | biological_process | carboxylic acid metabolic process |
A | 0019900 | molecular_function | kinase binding |
A | 0042802 | molecular_function | identical protein binding |
A | 0042867 | biological_process | pyruvate catabolic process |
A | 0045121 | cellular_component | membrane raft |
A | 0051287 | molecular_function | NAD binding |
A | 0070062 | cellular_component | extracellular exosome |
A | 1990204 | cellular_component | oxidoreductase complex |
B | 0003824 | molecular_function | catalytic activity |
B | 0004457 | molecular_function | lactate dehydrogenase activity |
B | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005743 | cellular_component | mitochondrial inner membrane |
B | 0005829 | cellular_component | cytosol |
B | 0006089 | biological_process | lactate metabolic process |
B | 0016020 | cellular_component | membrane |
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 | 0019674 | biological_process | NAD+ metabolic process |
B | 0019752 | biological_process | carboxylic acid metabolic process |
B | 0019900 | molecular_function | kinase binding |
B | 0042802 | molecular_function | identical protein binding |
B | 0042867 | biological_process | pyruvate catabolic process |
B | 0045121 | cellular_component | membrane raft |
B | 0051287 | molecular_function | NAD binding |
B | 0070062 | cellular_component | extracellular exosome |
B | 1990204 | cellular_component | oxidoreductase complex |
C | 0003824 | molecular_function | catalytic activity |
C | 0004457 | molecular_function | lactate dehydrogenase activity |
C | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005739 | cellular_component | mitochondrion |
C | 0005743 | cellular_component | mitochondrial inner membrane |
C | 0005829 | cellular_component | cytosol |
C | 0006089 | biological_process | lactate metabolic process |
C | 0016020 | cellular_component | membrane |
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 | 0019674 | biological_process | NAD+ metabolic process |
C | 0019752 | biological_process | carboxylic acid metabolic process |
C | 0019900 | molecular_function | kinase binding |
C | 0042802 | molecular_function | identical protein binding |
C | 0042867 | biological_process | pyruvate catabolic process |
C | 0045121 | cellular_component | membrane raft |
C | 0051287 | molecular_function | NAD binding |
C | 0070062 | cellular_component | extracellular exosome |
C | 1990204 | cellular_component | oxidoreductase complex |
D | 0003824 | molecular_function | catalytic activity |
D | 0004457 | molecular_function | lactate dehydrogenase activity |
D | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
D | 0005515 | molecular_function | protein binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005739 | cellular_component | mitochondrion |
D | 0005743 | cellular_component | mitochondrial inner membrane |
D | 0005829 | cellular_component | cytosol |
D | 0006089 | biological_process | lactate metabolic process |
D | 0016020 | cellular_component | membrane |
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 | 0019674 | biological_process | NAD+ metabolic process |
D | 0019752 | biological_process | carboxylic acid metabolic process |
D | 0019900 | molecular_function | kinase binding |
D | 0042802 | molecular_function | identical protein binding |
D | 0042867 | biological_process | pyruvate catabolic process |
D | 0045121 | cellular_component | membrane raft |
D | 0051287 | molecular_function | NAD binding |
D | 0070062 | cellular_component | extracellular exosome |
D | 1990204 | cellular_component | oxidoreductase complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NAD A 401 |
Chain | Residue |
A | GLY29 |
A | VAL98 |
A | ARG99 |
A | VAL116 |
A | ILE120 |
A | VAL136 |
A | SER137 |
A | ASN138 |
A | SER161 |
A | HIS193 |
A | THR248 |
A | GLN30 |
A | ILE252 |
A | OXQ402 |
A | HOH433 |
A | HOH434 |
A | VAL31 |
A | ASP52 |
A | VAL53 |
A | LEU54 |
A | TYR83 |
A | THR95 |
A | GLY97 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE OXQ A 402 |
Chain | Residue |
A | GLN100 |
A | ARG106 |
A | ASN138 |
A | LEU165 |
A | ARG169 |
A | HIS193 |
A | THR248 |
A | NAD401 |
site_id | AC3 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE NAD B 403 |
Chain | Residue |
B | VAL28 |
B | GLY29 |
B | GLN30 |
B | VAL31 |
B | ASP52 |
B | VAL53 |
B | LEU54 |
B | THR95 |
B | ALA96 |
B | GLY97 |
B | VAL98 |
B | ARG99 |
B | GLN100 |
B | ILE120 |
B | VAL136 |
B | SER137 |
B | ASN138 |
B | SER161 |
B | HIS193 |
B | THR248 |
B | ILE252 |
B | OXQ404 |
B | HOH424 |
B | HOH473 |
B | HOH480 |
D | ASN108 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE OXQ B 404 |
Chain | Residue |
B | GLN100 |
B | ARG106 |
B | ASN138 |
B | ARG169 |
B | HIS193 |
B | THR248 |
B | NAD403 |
B | HOH480 |
site_id | AC5 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE NAD C 405 |
Chain | Residue |
A | ASN108 |
C | VAL28 |
C | GLY29 |
C | GLN30 |
C | VAL31 |
C | ASP52 |
C | VAL53 |
C | LEU54 |
C | THR95 |
C | ALA96 |
C | GLY97 |
C | VAL98 |
C | ARG99 |
C | VAL116 |
C | VAL136 |
C | ASN138 |
C | SER161 |
C | HIS193 |
C | THR248 |
C | ILE252 |
C | OXQ406 |
C | HOH419 |
C | HOH427 |
C | HOH437 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE OXQ C 406 |
Chain | Residue |
C | GLN100 |
C | ARG106 |
C | ASN138 |
C | LEU165 |
C | ARG169 |
C | HIS193 |
C | ALA238 |
C | THR248 |
C | NAD405 |
C | HOH419 |
site_id | AC7 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NAD D 407 |
Chain | Residue |
D | GLY29 |
D | GLN30 |
D | VAL31 |
D | ASP52 |
D | VAL53 |
D | LEU54 |
D | THR95 |
D | ALA96 |
D | GLY97 |
D | VAL98 |
D | ARG99 |
D | VAL136 |
D | ASN138 |
D | SER161 |
D | LEU165 |
D | HIS193 |
D | THR248 |
D | ILE252 |
D | OXQ408 |
D | HOH419 |
D | HOH420 |
D | HOH443 |
D | HOH444 |
site_id | AC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE OXQ D 408 |
Chain | Residue |
D | GLN100 |
D | ARG106 |
D | ASN138 |
D | LEU165 |
D | ARG169 |
D | HIS193 |
D | ALA238 |
D | THR248 |
D | NAD407 |
D | HOH419 |
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 | LEU190-SER196 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | GLY194 | |
B | GLY194 | |
C | GLY194 | |
D | GLY194 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | VAL31 | |
B | VAL31 | |
C | VAL31 | |
D | VAL31 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11276087 |
Chain | Residue | Details |
A | GLN100 | |
B | GLN100 | |
C | GLN100 | |
D | GLN100 |
site_id | SWS_FT_FI4 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
A | LEU107 | |
C | PRO139 | |
C | PHE170 | |
C | ASN249 | |
D | LEU107 | |
D | PRO139 | |
D | PHE170 | |
D | ASN249 | |
A | PRO139 | |
A | PHE170 | |
A | ASN249 | |
B | LEU107 | |
B | PRO139 | |
B | PHE170 | |
B | ASN249 | |
C | LEU107 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: N-acetylalanine => ECO:0000269|Ref.4 |
Chain | Residue | Details |
A | THR2 | |
B | THR2 | |
C | THR2 | |
D | THR2 |
site_id | SWS_FT_FI6 |
Number of Residues | 16 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LEU7 | |
C | LEU58 | |
C | PHE119 | |
C | ASP329 | |
D | LEU7 | |
D | LEU58 | |
D | PHE119 | |
D | ASP329 | |
A | LEU58 | |
A | PHE119 | |
A | ASP329 | |
B | LEU7 | |
B | LEU58 | |
B | PHE119 | |
B | ASP329 | |
C | LEU7 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332 |
Chain | Residue | Details |
A | LEU44 | |
B | LEU44 | |
C | LEU44 | |
D | LEU44 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231 |
Chain | Residue | Details |
A | GLU240 | |
B | GLU240 | |
C | GLU240 | |
D | GLU240 |
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 |