5KKC
l-lactate dehydrogenase from rabbit muscle with the inhibitor 6DHNAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006089 | biological_process | lactate metabolic 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 (NAD+) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006089 | biological_process | lactate metabolic 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 (NAD+) activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006089 | biological_process | lactate metabolic 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 (NAD+) activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006089 | biological_process | lactate metabolic 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 | 27 |
| Details | binding site for residue 6V0 A 401 |
| Chain | Residue |
| A | GLY28 |
| A | ALA97 |
| A | ARG98 |
| A | GLN99 |
| A | ILE115 |
| A | ILE119 |
| A | VAL135 |
| A | SER136 |
| A | ASN137 |
| A | THR247 |
| A | ILE251 |
| A | ALA29 |
| A | HOH506 |
| A | HOH516 |
| A | HOH522 |
| A | HOH524 |
| A | HOH525 |
| A | HOH556 |
| A | HOH569 |
| A | HOH577 |
| A | VAL30 |
| A | ASP51 |
| A | VAL52 |
| A | MET53 |
| A | THR94 |
| A | ALA95 |
| A | GLY96 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 402 |
| Chain | Residue |
| A | GLU284 |
| A | ASP320 |
| B | HOH511 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 403 |
| Chain | Residue |
| A | ARG170 |
| A | HIS185 |
| A | HOH505 |
| A | HOH547 |
| A | HOH578 |
| D | HIS185 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | binding site for residue 6V0 B 401 |
| Chain | Residue |
| B | GLY28 |
| B | ALA29 |
| B | VAL30 |
| B | ASP51 |
| B | VAL52 |
| B | MET53 |
| B | THR94 |
| B | ALA95 |
| B | GLY96 |
| B | ARG98 |
| B | VAL135 |
| B | SER136 |
| B | ASN137 |
| B | SER160 |
| B | HIS192 |
| B | THR247 |
| B | ILE251 |
| B | HOH510 |
| B | HOH532 |
| B | HOH535 |
| B | HOH541 |
| B | HOH569 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 402 |
| Chain | Residue |
| B | ARG170 |
| B | HIS185 |
| B | HOH501 |
| B | HOH508 |
| B | HOH509 |
| B | HOH585 |
| C | HIS185 |
| site_id | AC6 |
| Number of Residues | 28 |
| Details | binding site for residue 6V0 C 401 |
| Chain | Residue |
| C | GLY28 |
| C | ALA29 |
| C | VAL30 |
| C | ASP51 |
| C | VAL52 |
| C | MET53 |
| C | LYS56 |
| C | THR94 |
| C | ALA95 |
| C | GLY96 |
| C | ALA97 |
| C | ARG98 |
| C | ILE115 |
| C | ILE119 |
| C | VAL135 |
| C | ASN137 |
| C | SER160 |
| C | LEU164 |
| C | HIS192 |
| C | THR247 |
| C | ILE251 |
| C | HOH516 |
| C | HOH518 |
| C | HOH521 |
| C | HOH522 |
| C | HOH523 |
| C | HOH543 |
| C | HOH569 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 C 402 |
| Chain | Residue |
| B | HIS185 |
| C | ARG170 |
| C | HIS185 |
| C | HOH509 |
| C | HOH524 |
| C | HOH527 |
| site_id | AC8 |
| Number of Residues | 28 |
| Details | binding site for residue 6V0 D 401 |
| Chain | Residue |
| D | GLY26 |
| D | VAL27 |
| D | GLY28 |
| D | ALA29 |
| D | VAL30 |
| D | ASP51 |
| D | VAL52 |
| D | THR94 |
| D | ALA95 |
| D | GLY96 |
| D | ALA97 |
| D | ARG98 |
| D | LEU108 |
| D | ILE115 |
| D | ILE119 |
| D | VAL135 |
| D | ASN137 |
| D | SER160 |
| D | LEU164 |
| D | HIS192 |
| D | THR247 |
| D | ILE251 |
| D | HOH505 |
| D | HOH523 |
| D | HOH528 |
| D | HOH537 |
| D | HOH547 |
| D | HOH548 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 D 402 |
| Chain | Residue |
| A | HIS185 |
| D | ARG170 |
| D | HIS185 |
| D | HOH510 |
| D | HOH524 |
| D | HOH530 |
| D | HOH583 |
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 | LEU189-SER195 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"19715328","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 131 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"P00338","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P00338","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P00338","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P04642","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00338","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P00338","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
