9LDB
DESIGN AND SYNTHESIS OF NEW ENZYMES BASED ON THE LACTATE DEHYDROGENASE FRAMEWORK
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 | 0005739 | cellular_component | mitochondrion |
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 |
A | 0042802 | molecular_function | identical protein binding |
A | 1990204 | cellular_component | oxidoreductase complex |
B | 0003824 | molecular_function | catalytic activity |
B | 0004459 | molecular_function | L-lactate dehydrogenase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
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 |
B | 0042802 | molecular_function | identical protein binding |
B | 1990204 | cellular_component | oxidoreductase complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 402 |
Chain | Residue |
A | ARG109 |
A | ASN140 |
A | ARG171 |
A | HIS195 |
A | ALA236 |
A | THR246 |
A | NAD401 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 403 |
Chain | Residue |
A | HIS188 |
A | HOH430 |
A | HOH433 |
A | HOH446 |
A | HOH450 |
A | ARG173 |
A | HIS188 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 B 403 |
Chain | Residue |
B | ARG173 |
B | HIS188 |
B | HIS188 |
B | HOH442 |
B | HOH444 |
B | HOH462 |
B | HOH463 |
site_id | AC4 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE NAD A 401 |
Chain | Residue |
A | GLY30 |
A | ALA31 |
A | VAL32 |
A | ASP53 |
A | VAL54 |
A | MET55 |
A | THR97 |
A | ALA98 |
A | GLY99 |
A | ALA100 |
A | ARG101 |
A | PHE122 |
A | ILE123 |
A | VAL138 |
A | ASN140 |
A | SER163 |
A | LEU167 |
A | HIS195 |
A | THR246 |
A | ILE250 |
A | SO4402 |
A | HOH404 |
A | HOH411 |
A | HOH413 |
A | HOH424 |
A | HOH429 |
A | HOH442 |
A | HOH464 |
B | HOH425 |
B | HOH473 |
site_id | AC5 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE NAD B 401 |
Chain | Residue |
B | GLY30 |
B | ALA31 |
B | VAL32 |
B | ASP53 |
B | VAL54 |
B | MET55 |
B | THR97 |
B | ALA98 |
B | GLY99 |
B | ALA100 |
B | ARG101 |
B | ILE119 |
B | VAL138 |
B | ASN140 |
B | SER163 |
B | HIS195 |
B | THR246 |
B | ILE250 |
B | OXM402 |
B | HOH407 |
B | HOH414 |
B | HOH416 |
B | HOH429 |
B | HOH441 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE OXM B 402 |
Chain | Residue |
B | GLN102 |
B | ARG109 |
B | ASN140 |
B | ARG171 |
B | HIS195 |
B | ALA236 |
B | THR246 |
B | NAD401 |
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 | LEU192-SER198 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | GLY196 | |
B | GLY196 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:1678537 |
Chain | Residue | Details |
A | ALA31 | |
A | GLN102 | |
B | ALA31 | |
B | GLN102 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: |
Chain | Residue | Details |
A | LEU110 | |
A | PRO141 | |
A | PHE172 | |
A | SER247 | |
B | LEU110 | |
B | PRO141 | |
B | PHE172 | |
B | SER247 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylalanine => ECO:0000269|PubMed:838465 |
Chain | Residue | Details |
A | THR2 | |
B | THR2 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 |
Chain | Residue | Details |
A | ASP5 | |
A | PHE122 | |
A | SER318 | |
B | ASP5 | |
B | PHE122 | |
B | SER318 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P00338 |
Chain | Residue | Details |
A | GLU14 | |
A | ASP84 | |
A | TYR130 | |
B | GLU14 | |
B | ASP84 | |
B | TYR130 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P00338 |
Chain | Residue | Details |
A | LEU59 | |
B | LEU59 |
site_id | SWS_FT_FI8 |
Number of Residues | 6 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P06151 |
Chain | Residue | Details |
A | GLU223 | |
A | GLU231 | |
A | LEU242 | |
B | GLU223 | |
B | GLU231 | |
B | LEU242 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P06151 |
Chain | Residue | Details |
A | GLU238 | |
B | GLU238 |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04642 |
Chain | Residue | Details |
A | PRO309 | |
A | LEU322 | |
B | PRO309 | |
B | LEU322 |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P00338 |
Chain | Residue | Details |
A | LEU59 | |
B | LEU59 |