3DDN
Crystal structure of hydroxypyruvic acid phosphate bound D-3-phosphoglycerate dehydrogenase in mycobacterium tuberculosis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004617 | molecular_function | phosphoglycerate dehydrogenase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006564 | biological_process | L-serine biosynthetic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009274 | cellular_component | peptidoglycan-based cell wall |
| 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 |
| A | 0120568 | molecular_function | (R)-2-hydroxyglutarate (NAD+) dehydrogenase activity |
| B | 0004617 | molecular_function | phosphoglycerate dehydrogenase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006564 | biological_process | L-serine biosynthetic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009274 | cellular_component | peptidoglycan-based cell wall |
| 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 |
| B | 0120568 | molecular_function | (R)-2-hydroxyglutarate (NAD+) dehydrogenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE TLA A 530 |
| Chain | Residue |
| A | ARG446 |
| A | HIS447 |
| A | HOH788 |
| B | LYS439 |
| B | ASP449 |
| B | LEU450 |
| B | ARG451 |
| B | ARG501 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE TLA B 530 |
| Chain | Residue |
| A | ASP449 |
| A | LEU450 |
| A | ARG451 |
| A | ALA484 |
| A | ARG501 |
| B | ARG446 |
| B | HIS447 |
| B | SER488 |
| B | GLU489 |
| A | LYS439 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE TLA B 531 |
| Chain | Residue |
| B | GLU361 |
| B | GLU363 |
| B | LYS402 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE HPV B 600 |
| Chain | Residue |
| A | ARG132 |
| B | SER52 |
| B | ARG72 |
| B | GLY76 |
| B | ASN99 |
| B | ALA283 |
| B | GLN289 |
| B | HOH730 |
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. VGVVGlGRIGqlvaqriaafgay.VVaYD |
| Chain | Residue | Details |
| A | VAL145-ASP172 |
| site_id | PS00670 |
| Number of Residues | 23 |
| Details | D_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. LLarADFIsVHlPktpeTagLiD |
| Chain | Residue | Details |
| A | LEU193-ASP215 |
| site_id | PS00671 |
| Number of Residues | 17 |
| Details | D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. TKpGvIIVNaARGgLVD |
| Chain | Residue | Details |
| A | THR222-ASP238 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 144 |
| Details | Domain: {"description":"ACT","evidences":[{"source":"PROSITE-ProRule","id":"PRU01007","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P0A9T0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1gdh |
| Chain | Residue | Details |
| A | HIS280 | |
| A | ASP257 | |
| A | GLU262 | |
| A | ARG233 | |
| A | GLY235 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1gdh |
| Chain | Residue | Details |
| B | HIS280 | |
| B | ASP257 | |
| B | GLU262 | |
| B | ARG233 | |
| B | GLY235 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1gdh |
| Chain | Residue | Details |
| A | HIS280 | |
| A | GLU262 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1gdh |
| Chain | Residue | Details |
| B | HIS280 | |
| B | GLU262 |
