6DQG
Human glutamate dehydrogenase, H454Y mutant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
| E | 0006520 | biological_process | amino acid metabolic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
| F | 0006520 | biological_process | amino acid metabolic process |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 A 1001 |
| Chain | Residue |
| A | ARG463 |
| A | HOH1102 |
| A | HOH1103 |
| B | SER397 |
| B | HOH709 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue PO4 B 601 |
| Chain | Residue |
| B | HIS213 |
| B | LYS450 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 B 602 |
| Chain | Residue |
| B | ARG269 |
| B | TYR454 |
| B | ARG265 |
| B | TYR266 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 C 601 |
| Chain | Residue |
| C | SER217 |
| C | ARG221 |
| C | ARG265 |
| C | TYR266 |
| C | ARG269 |
| C | LYS450 |
| C | TYR454 |
| C | HOH710 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 C 602 |
| Chain | Residue |
| C | HIS213 |
| C | LYS391 |
| C | HOH721 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 D 601 |
| Chain | Residue |
| D | ILE207 |
| D | HIS213 |
| D | GLY214 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 D 602 |
| Chain | Residue |
| D | ARG221 |
| D | ARG265 |
| D | TYR266 |
| D | ARG269 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 D 603 |
| Chain | Residue |
| C | ASP123 |
| C | ARG463 |
| C | HOH727 |
| D | SER397 |
| D | ARG400 |
| D | HOH708 |
| D | HOH733 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue PO4 E 601 |
| Chain | Residue |
| E | HIS213 |
| E | GLY214 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 E 602 |
| Chain | Residue |
| E | ARG221 |
| E | ARG265 |
| E | TYR266 |
| E | ARG269 |
| E | TYR454 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 E 603 |
| Chain | Residue |
| D | ARG463 |
| E | SER397 |
| E | ARG400 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 F 2001 |
| Chain | Residue |
| F | HIS213 |
| F | GLY214 |
| F | LYS450 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 F 2002 |
| Chain | Residue |
| F | SER217 |
| F | ARG221 |
| F | ARG265 |
| F | TYR266 |
| F | ARG269 |
| F | LYS450 |
| F | TYR454 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 F 2003 |
| Chain | Residue |
| B | ARG463 |
| F | HIS213 |
| F | LYS391 |
| F | SER397 |
| F | HOH2102 |
| F | HOH2119 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 F 2004 |
| Chain | Residue |
| A | SER397 |
| A | ARG400 |
| F | ASP123 |
| F | ARG463 |
| F | HOH2123 |
| F | HOH2127 |
Functional Information from PROSITE/UniProt
| site_id | PS00074 |
| Number of Residues | 14 |
| Details | GLFV_DEHYDROGENASE Glu / Leu / Phe / Val dehydrogenases active site. VpfGGAKaGvkiNP |
| Chain | Residue | Details |
| A | VAL124-PRO137 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10011","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 84 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00366","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 54 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P00366","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"29192674","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 30 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"ADP-ribosylcysteine","evidences":[{"source":"PubMed","id":"16023112","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 48 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P00366","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P10860","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
