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 | 0004457 | molecular_function | lactate dehydrogenase activity |
| A | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| 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 | 0019661 | biological_process | glucose catabolic process to lactate via pyruvate |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0035686 | cellular_component | sperm fibrous sheath |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042867 | biological_process | pyruvate catabolic process |
| 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 | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| 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 | 0019661 | biological_process | glucose catabolic process to lactate via pyruvate |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0035686 | cellular_component | sperm fibrous sheath |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042867 | biological_process | pyruvate catabolic process |
| 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 | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 58 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"1678537","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"838465","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P00338","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P00338","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P04642","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| 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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | HIS195 | |
| A | ASP168 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | HIS195 | |
| B | ASP168 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | HIS195 | |
| A | ARG171 | |
| A | ASP168 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | HIS195 | |
| B | ARG171 | |
| B | ASP168 |
