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 activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006089 | biological_process | lactate metabolic process |
A | 0006090 | biological_process | pyruvate 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 activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006089 | biological_process | lactate metabolic process |
B | 0006090 | biological_process | pyruvate 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 activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0006089 | biological_process | lactate metabolic process |
C | 0006090 | biological_process | pyruvate 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 activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0006089 | biological_process | lactate metabolic process |
D | 0006090 | biological_process | pyruvate 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 | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:19715328 |
Chain | Residue | Details |
A | HIS192 | |
B | HIS192 | |
C | HIS192 | |
D | HIS192 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY28 | |
B | ASN137 | |
B | ARG168 | |
B | THR247 | |
C | GLY28 | |
C | ARG98 | |
C | ARG105 | |
C | ASN137 | |
C | ARG168 | |
C | THR247 | |
D | GLY28 | |
A | ARG98 | |
D | ARG98 | |
D | ARG105 | |
D | ASN137 | |
D | ARG168 | |
D | THR247 | |
A | ARG105 | |
A | ASN137 | |
A | ARG168 | |
A | THR247 | |
B | GLY28 | |
B | ARG98 | |
B | ARG105 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P00338 |
Chain | Residue | Details |
A | ALA1 | |
B | ALA1 | |
C | ALA1 | |
D | ALA1 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 |
Chain | Residue | Details |
A | LYS4 | |
D | LYS4 | |
D | LYS117 | |
D | LYS317 | |
A | LYS117 | |
A | LYS317 | |
B | LYS4 | |
B | LYS117 | |
B | LYS317 | |
C | LYS4 | |
C | LYS117 | |
C | LYS317 |
site_id | SWS_FT_FI5 |
Number of Residues | 12 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P00338 |
Chain | Residue | Details |
A | LYS13 | |
D | LYS13 | |
D | LYS80 | |
D | LYS125 | |
A | LYS80 | |
A | LYS125 | |
B | LYS13 | |
B | LYS80 | |
B | LYS125 | |
C | LYS13 | |
C | LYS80 | |
C | LYS125 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P00338 |
Chain | Residue | Details |
A | LYS56 | |
B | LYS56 | |
C | LYS56 | |
D | LYS56 |
site_id | SWS_FT_FI7 |
Number of Residues | 12 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P06151 |
Chain | Residue | Details |
A | LYS223 | |
D | LYS223 | |
D | LYS231 | |
D | LYS242 | |
A | LYS231 | |
A | LYS242 | |
B | LYS223 | |
B | LYS231 | |
B | LYS242 | |
C | LYS223 | |
C | LYS231 | |
C | LYS242 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P06151 |
Chain | Residue | Details |
A | TYR238 | |
B | TYR238 | |
C | TYR238 | |
D | TYR238 |
site_id | SWS_FT_FI9 |
Number of Residues | 8 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04642 |
Chain | Residue | Details |
A | THR308 | |
A | THR321 | |
B | THR308 | |
B | THR321 | |
C | THR308 | |
C | THR321 | |
D | THR308 | |
D | THR321 |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00338 |
Chain | Residue | Details |
A | SER309 | |
B | SER309 | |
C | SER309 | |
D | SER309 |
site_id | SWS_FT_FI11 |
Number of Residues | 8 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P00338 |
Chain | Residue | Details |
A | LYS56 | |
B | LYS56 | |
C | LYS56 | |
D | LYS56 |