1J4A
INSIGHTS INTO DOMAIN CLOSURE, SUBSTRATE SPECIFICITY AND CATALYSIS OF D-LACTATE DEHYDROGENASE FROM LACTOBACILLUS BULGARICUS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006089 | biological_process | lactate metabolic process |
| A | 0008720 | molecular_function | D-lactate dehydrogenase (NAD+) activity |
| 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 | 0051287 | molecular_function | NAD binding |
| B | 0006089 | biological_process | lactate metabolic process |
| B | 0008720 | molecular_function | D-lactate dehydrogenase (NAD+) activity |
| 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 | 0051287 | molecular_function | NAD binding |
| C | 0006089 | biological_process | lactate metabolic process |
| C | 0008720 | molecular_function | D-lactate dehydrogenase (NAD+) activity |
| 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 | 0051287 | molecular_function | NAD binding |
| D | 0006089 | biological_process | lactate metabolic process |
| D | 0008720 | molecular_function | D-lactate dehydrogenase (NAD+) activity |
| 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 | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1400 |
| Chain | Residue |
| A | GLY155 |
| A | HIS156 |
| A | ILE157 |
| A | HOH1423 |
| A | HOH1444 |
| A | HOH1479 |
| A | HOH1642 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1401 |
| Chain | Residue |
| A | VAL79 |
| A | GLY80 |
| A | HOH1611 |
| A | GLN55 |
| A | ASN78 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1402 |
| Chain | Residue |
| A | ARG236 |
| A | GLY237 |
| A | VAL261 |
| A | LYS297 |
| A | HOH1470 |
| A | HOH1554 |
| A | HOH1638 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1403 |
| Chain | Residue |
| A | LYS18 |
| A | GLU21 |
| A | TYR31 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2400 |
| Chain | Residue |
| B | GLY155 |
| B | HIS156 |
| B | ILE157 |
| B | HOH2416 |
| B | HOH2488 |
| B | HOH2585 |
| B | HOH2656 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2401 |
| Chain | Residue |
| B | ASN78 |
| B | VAL79 |
| B | GLY80 |
| B | SO42403 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2402 |
| Chain | Residue |
| B | HIS304 |
| B | ASN308 |
| B | HOH2511 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2403 |
| Chain | Residue |
| B | TYR53 |
| B | PHE300 |
| B | SO42401 |
| B | HOH2495 |
| B | HOH2572 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 C 3400 |
| Chain | Residue |
| C | GLY155 |
| C | HIS156 |
| C | ILE157 |
| C | HOH3415 |
| C | HOH3467 |
| C | HOH3530 |
| C | HOH3554 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D 4400 |
| Chain | Residue |
| D | GLY155 |
| D | HIS156 |
| D | ILE157 |
| D | HOH4418 |
| D | HOH4449 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 4401 |
| Chain | Residue |
| D | GLN55 |
| D | ASN78 |
| D | VAL79 |
| D | GLY80 |
| D | HOH4535 |
| D | HOH4626 |
Functional Information from PROSITE/UniProt
| site_id | PS00065 |
| Number of Residues | 28 |
| Details | D_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. VGVVGtGHIGqvfmqimegfgak.VItYD |
| Chain | Residue | Details |
| A | VAL149-ASP176 |
| site_id | PS00670 |
| Number of Residues | 23 |
| Details | D_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. LYkqADVIsLHvPdvpaNvhMiN |
| Chain | Residue | Details |
| A | LEU196-ASN218 |
| site_id | PS00671 |
| Number of Residues | 17 |
| Details | D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MKqDvVIVNvSRGpLVD |
| Chain | Residue | Details |
| A | MET225-ASP241 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"9063466","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"9063466","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12054772","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1J49","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12054772","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12054772","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1j49 |
| Chain | Residue | Details |
| A | ARG236 | |
| A | ASP209 | |
| A | GLU265 | |
| A | LYS297 | |
| A | ASP260 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1j49 |
| Chain | Residue | Details |
| B | ARG236 | |
| B | ASP209 | |
| B | GLU265 | |
| B | LYS297 | |
| B | ASP260 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1j49 |
| Chain | Residue | Details |
| C | ARG236 | |
| C | ASP209 | |
| C | GLU265 | |
| C | LYS297 | |
| C | ASP260 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1j49 |
| Chain | Residue | Details |
| D | ARG236 | |
| D | ASP209 | |
| D | GLU265 | |
| D | LYS297 | |
| D | ASP260 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 576 |
| Chain | Residue | Details |
| A | ARG236 | electrostatic stabiliser |
| A | ASP260 | steric role |
| A | GLU265 | electrostatic stabiliser |
| A | LYS297 | proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 576 |
| Chain | Residue | Details |
| B | ARG236 | electrostatic stabiliser |
| B | ASP260 | steric role |
| B | GLU265 | electrostatic stabiliser |
| B | LYS297 | proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 576 |
| Chain | Residue | Details |
| C | ARG236 | electrostatic stabiliser |
| C | ASP260 | steric role |
| C | GLU265 | electrostatic stabiliser |
| C | LYS297 | proton acceptor, proton donor |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 576 |
| Chain | Residue | Details |
| D | ARG236 | electrostatic stabiliser |
| D | ASP260 | steric role |
| D | GLU265 | electrostatic stabiliser |
| D | LYS297 | proton acceptor, proton donor |
