1P43
REVERSE PROTONATION IS THE KEY TO GENERAL ACID-BASE CATALYSIS IN ENOLASE
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 |
| B | 0000015 | cellular_component | phosphopyruvate hydratase complex |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0000324 | cellular_component | fungal-type vacuole |
| B | 0004634 | molecular_function | phosphopyruvate hydratase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006096 | biological_process | glycolytic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0032889 | biological_process | regulation of vacuole fusion, non-autophagic |
| B | 0046872 | molecular_function | metal ion binding |
| B | 1904408 | molecular_function | melatonin binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 438 |
| Chain | Residue |
| A | ASP246 |
| A | GLU295 |
| A | ASP320 |
| A | 2PG441 |
| A | HOH1002 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 439 |
| Chain | Residue |
| A | HOH1003 |
| A | HOH1867 |
| A | SER39 |
| A | ASP321 |
| A | 2PG441 |
| A | HOH1001 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 938 |
| Chain | Residue |
| B | ASP746 |
| B | GLU795 |
| B | ASP820 |
| B | 2PG941 |
| B | HOH1007 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 939 |
| Chain | Residue |
| B | SER539 |
| B | 2PG941 |
| B | HOH1005 |
| B | HOH1006 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 2PG A 441 |
| Chain | Residue |
| A | GLY37 |
| A | ALA38 |
| A | GLN168 |
| A | GLU211 |
| A | ASP246 |
| A | GLU295 |
| A | ASP320 |
| A | LEU343 |
| A | LYS345 |
| A | HIS373 |
| A | ARG374 |
| A | SER375 |
| A | LYS396 |
| A | MG438 |
| A | MG439 |
| A | HOH1003 |
| A | HOH1867 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE 2PG B 941 |
| Chain | Residue |
| B | GLY537 |
| B | ALA538 |
| B | GLN668 |
| B | GLU711 |
| B | ASP746 |
| B | GLU795 |
| B | ASP820 |
| B | LEU843 |
| B | LYS845 |
| B | HIS873 |
| B | ARG874 |
| B | SER875 |
| B | LYS896 |
| B | MG938 |
| B | MG939 |
| B | HOH1006 |
| B | HOH1050 |
| B | HOH1515 |
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 | 2 |
| 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 | 2 |
| 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 | 10 |
| 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 | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8605183","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| 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 | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00925","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P00925","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| 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 | 4 |
| 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 | 4 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| A | GLU211 | |
| A | HIS373 | |
| A | LYS396 | |
| A | GLN168 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| B | GLN668 | |
| B | LYS896 | |
| B | GLU711 | |
| B | HIS873 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| A | LYS345 | |
| A | GLU211 | |
| A | HIS373 | |
| A | GLN168 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| B | GLN668 | |
| B | LYS845 | |
| B | GLU711 | |
| B | HIS873 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| A | LYS345 | |
| A | HIS191 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| B | HIS691 | |
| B | LYS845 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| A | LYS242 | |
| A | LYS345 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| B | LYS845 | |
| B | LYS742 |
| 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 | GLN168 | 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 |
| site_id | MCSA2 |
| Number of Residues | 10 |
| Details | M-CSA 311 |
| Chain | Residue | Details |
| B | SER539 | metal ligand |
| B | LYS896 | electrostatic stabiliser, hydrogen bond donor, proton shuttle (general acid/base) |
| B | HIS659 | electrostatic stabiliser, proton shuttle (general acid/base) |
| B | GLN668 | activator, electrostatic stabiliser, hydrogen bond acceptor, increase acidity, repulsive charge-charge interaction |
| B | GLU711 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor |
| B | ASP746 | metal ligand |
| B | GLU795 | metal ligand |
| B | ASP820 | metal ligand |
| B | LYS845 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor |
| B | HIS873 | electrostatic stabiliser, hydrogen bond donor |
