5IDZ
Structure of Human Enolase 2 in complex with (S)-(1-hydroxy-2-oxopiperidin-3-yl)phosphonate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000015 | cellular_component | phosphopyruvate hydratase complex |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0001917 | cellular_component | photoreceptor inner segment |
| A | 0004634 | molecular_function | phosphopyruvate hydratase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005938 | cellular_component | cell cortex |
| A | 0006094 | biological_process | gluconeogenesis |
| A | 0006096 | biological_process | glycolytic process |
| A | 0009410 | biological_process | response to xenobiotic stimulus |
| A | 0009986 | cellular_component | cell surface |
| A | 0016020 | cellular_component | membrane |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019899 | molecular_function | enzyme binding |
| A | 0030426 | cellular_component | growth cone |
| A | 0032355 | biological_process | response to estradiol |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043025 | cellular_component | neuronal cell body |
| A | 0043204 | cellular_component | perikaryon |
| A | 0044877 | molecular_function | protein-containing complex binding |
| A | 0045121 | cellular_component | membrane raft |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0061621 | biological_process | canonical glycolysis |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0097060 | cellular_component | synaptic membrane |
| B | 0000015 | cellular_component | phosphopyruvate hydratase complex |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0001917 | cellular_component | photoreceptor inner segment |
| B | 0004634 | molecular_function | phosphopyruvate hydratase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0005938 | cellular_component | cell cortex |
| B | 0006094 | biological_process | gluconeogenesis |
| B | 0006096 | biological_process | glycolytic process |
| B | 0009410 | biological_process | response to xenobiotic stimulus |
| B | 0009986 | cellular_component | cell surface |
| B | 0016020 | cellular_component | membrane |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019899 | molecular_function | enzyme binding |
| B | 0030426 | cellular_component | growth cone |
| B | 0032355 | biological_process | response to estradiol |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0043025 | cellular_component | neuronal cell body |
| B | 0043204 | cellular_component | perikaryon |
| B | 0044877 | molecular_function | protein-containing complex binding |
| B | 0045121 | cellular_component | membrane raft |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0061621 | biological_process | canonical glycolysis |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0097060 | cellular_component | synaptic membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 500 |
| Chain | Residue |
| A | ASP245 |
| A | GLU293 |
| A | ASP318 |
| A | 6BM501 |
| A | HOH623 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue 6BM A 501 |
| Chain | Residue |
| A | GLU293 |
| A | ASP318 |
| A | LEU341 |
| A | LYS343 |
| A | HIS371 |
| A | ARG372 |
| A | SER373 |
| A | LYS394 |
| A | MG500 |
| A | HOH623 |
| A | ALA39 |
| A | GLN166 |
| A | GLU167 |
| A | ASP245 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue PGE A 502 |
| Chain | Residue |
| A | LYS5 |
| A | TYR25 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 500 |
| Chain | Residue |
| B | ASP245 |
| B | GLU293 |
| B | ASP318 |
| B | 6BM501 |
| B | HOH633 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | binding site for residue 6BM B 501 |
| Chain | Residue |
| B | ALA39 |
| B | GLN166 |
| B | GLU167 |
| B | ASP245 |
| B | GLU293 |
| B | ASP318 |
| B | LEU341 |
| B | LYS343 |
| B | HIS371 |
| B | ARG372 |
| B | SER373 |
| B | LYS394 |
| B | MG500 |
| B | HOH633 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue PGE B 502 |
| Chain | Residue |
| B | LYS5 |
| B | TRP7 |
| B | TYR25 |
Functional Information from PROSITE/UniProt
| site_id | PS00164 |
| Number of Residues | 14 |
| Details | ENOLASE Enolase signature. LLLKvNQIGSVTEA |
| Chain | Residue | Details |
| A | LEU340-ALA353 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P00924","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P00924","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P06733","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00924","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"UniProtKB","id":"P06733","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P06733","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P17182","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P17183","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P17182","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P06733","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P06733","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P06733","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P17182","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P06733","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
