1ELS
CATALYTIC METAL ION BINDING IN ENOLASE: THE CRYSTAL STRUCTURE OF ENOLASE-MN2+-PHOSPHONOACETOHYDROXAMATE COMPLEX AT 2.4 ANGSTROMS RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000015 | cellular_component | phosphopyruvate hydratase complex |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0000324 | cellular_component | fungal-type vacuole |
| A | 0004634 | molecular_function | phosphopyruvate hydratase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006096 | biological_process | glycolytic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0032889 | biological_process | regulation of vacuole fusion, non-autophagic |
| A | 0046872 | molecular_function | metal ion binding |
| A | 1904408 | molecular_function | melatonin binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 438 |
| Chain | Residue |
| A | ASP246 |
| A | GLU295 |
| A | ASP320 |
| A | PAH439 |
| A | HOH527 |
| A | HOH653 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN A 440 |
| Chain | Residue |
| A | GLY37 |
| A | ALA38 |
| A | SER375 |
| A | PAH439 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PAH A 439 |
| Chain | Residue |
| A | GLY37 |
| A | SER39 |
| A | GLN167 |
| A | GLU168 |
| A | ASP246 |
| A | ASP320 |
| A | LYS345 |
| A | ARG374 |
| A | SER375 |
| A | LYS396 |
| A | MN438 |
| A | MN440 |
| A | HOH525 |
| A | HOH653 |
| A | HOH674 |
| A | HOH730 |
| A | HOH768 |
| site_id | CAT |
| Number of Residues | 5 |
| Details | ACTIVE SITE RESIDUES THAT ARE PROBABLY INVOLVED IN SUBSTRATE BINDING AND CATALYSIS |
| Chain | Residue |
| A | LYS345 |
| A | HIS373 |
| A | LYS396 |
| A | GLU168 |
| A | GLU211 |
| site_id | ME1 |
| Number of Residues | 3 |
| Details | METAL IONS BINDING SITE |
| Chain | Residue |
| A | ASP246 |
| A | GLU295 |
| A | ASP320 |
| site_id | PHO |
| Number of Residues | 4 |
| Details | PHOSPHATE GROUP BINDING SITE |
| Chain | Residue |
| A | ALA38 |
| A | HIS159 |
| A | LYS345 |
| A | SER375 |
Functional Information from PROSITE/UniProt
| site_id | PS00164 |
| Number of Residues | 14 |
| Details | ENOLASE Enolase signature. LLLKvNQIGTLSES |
| Chain | Residue | Details |
| A | LEU342-SER355 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"12846578","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"12846578","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8634301","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8605183","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9376357","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8605183","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12054465","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8605183","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9376357","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00925","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P00925","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P00925","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 9790688, 8193144 |
| Chain | Residue | Details |
| A | HIS159 | |
| A | LYS396 |
| site_id | MCSA1 |
| Number of Residues | 10 |
| Details | M-CSA 311 |
| Chain | Residue | Details |
| A | SER39 | metal ligand |
| A | LYS396 | electrostatic stabiliser, hydrogen bond donor, proton shuttle (general acid/base) |
| A | HIS159 | electrostatic stabiliser, proton shuttle (general acid/base) |
| A | GLU168 | activator, electrostatic stabiliser, hydrogen bond acceptor, increase acidity, repulsive charge-charge interaction |
| A | GLU211 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor |
| A | ASP246 | metal ligand |
| A | GLU295 | metal ligand |
| A | ASP320 | metal ligand |
| A | LYS345 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor |
| A | HIS373 | electrostatic stabiliser, hydrogen bond donor |
