1L8P
Mg-phosphonoacetohydroxamate complex of S39A yeast enolase 1
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 | 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 | 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 |
C | 0000015 | cellular_component | phosphopyruvate hydratase complex |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0000324 | cellular_component | fungal-type vacuole |
C | 0004634 | molecular_function | phosphopyruvate hydratase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0005739 | cellular_component | mitochondrion |
C | 0005829 | cellular_component | cytosol |
C | 0005886 | cellular_component | plasma membrane |
C | 0006096 | biological_process | glycolytic process |
C | 0016829 | molecular_function | lyase activity |
C | 0032889 | biological_process | regulation of vacuole fusion, non-autophagic |
C | 0046872 | molecular_function | metal ion binding |
C | 1904408 | molecular_function | melatonin binding |
D | 0000015 | cellular_component | phosphopyruvate hydratase complex |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0000324 | cellular_component | fungal-type vacuole |
D | 0004634 | molecular_function | phosphopyruvate hydratase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0005739 | cellular_component | mitochondrion |
D | 0005829 | cellular_component | cytosol |
D | 0005886 | cellular_component | plasma membrane |
D | 0006096 | biological_process | glycolytic process |
D | 0016829 | molecular_function | lyase activity |
D | 0032889 | biological_process | regulation of vacuole fusion, non-autophagic |
D | 0046872 | molecular_function | metal ion binding |
D | 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 | PAH440 |
A | HOH2011 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 439 |
Chain | Residue |
A | HOH2010 |
A | PAH440 |
A | HOH2007 |
A | HOH2008 |
A | HOH2009 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 938 |
Chain | Residue |
B | ASP746 |
B | GLU795 |
B | ASP820 |
B | PAH940 |
B | HOH2016 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 939 |
Chain | Residue |
B | PAH940 |
B | HOH2012 |
B | HOH2013 |
B | HOH2014 |
B | HOH2015 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 1438 |
Chain | Residue |
C | PAH1440 |
C | HOH2024 |
C | HOH2025 |
C | HOH2026 |
C | HOH2027 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 1439 |
Chain | Residue |
C | ASP1246 |
C | GLU1295 |
C | ASP1320 |
C | PAH1440 |
C | HOH2028 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 1938 |
Chain | Residue |
D | PAH1940 |
D | HOH2019 |
D | HOH2020 |
D | HOH2021 |
D | HOH2022 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 1939 |
Chain | Residue |
D | ASP1746 |
D | GLU1795 |
D | ASP1820 |
D | PAH1940 |
D | HOH2023 |
site_id | AC9 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE PAH A 440 |
Chain | Residue |
A | GLY37 |
A | ALA38 |
A | GLN167 |
A | GLU168 |
A | ASP246 |
A | GLU295 |
A | ASP320 |
A | LEU343 |
A | LYS345 |
A | ARG374 |
A | SER375 |
A | LYS396 |
A | MG438 |
A | MG439 |
A | HOH2004 |
A | HOH2007 |
A | HOH2008 |
A | HOH2009 |
A | HOH2853 |
site_id | BC1 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE PAH B 940 |
Chain | Residue |
B | GLY537 |
B | ALA538 |
B | GLN667 |
B | GLU668 |
B | ASP746 |
B | GLU795 |
B | ASP820 |
B | LEU843 |
B | LYS845 |
B | ARG874 |
B | SER875 |
B | LYS896 |
B | MG938 |
B | MG939 |
B | HOH2012 |
B | HOH2015 |
B | HOH2018 |
B | HOH2827 |
site_id | BC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE PAH C 1440 |
Chain | Residue |
C | GLY1037 |
C | ALA1038 |
C | GLN1167 |
C | GLU1168 |
C | ASP1246 |
C | GLU1295 |
C | ASP1320 |
C | LEU1343 |
C | LYS1345 |
C | ARG1374 |
C | SER1375 |
C | LYS1396 |
C | MG1438 |
C | MG1439 |
C | HOH2024 |
C | HOH2025 |
C | HOH2026 |
C | HOH2029 |
C | HOH2603 |
site_id | BC3 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE PAH D 1940 |
Chain | Residue |
D | GLU1668 |
D | ASP1746 |
D | GLU1795 |
D | ASP1820 |
D | LEU1843 |
D | LYS1845 |
D | ARG1874 |
D | SER1875 |
D | LYS1896 |
D | MG1938 |
D | MG1939 |
D | HOH2021 |
D | HOH2022 |
D | HOH2382 |
D | HOH2844 |
D | GLY1537 |
D | ALA1538 |
D | GLN1667 |
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 | 4 |
Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:12846578 |
Chain | Residue | Details |
A | GLY212 | |
B | GLY712 | |
C | GLY1212 | |
D | GLY1712 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:12846578, ECO:0000269|PubMed:8634301 |
Chain | Residue | Details |
A | VAL346 | |
B | VAL846 | |
C | VAL1346 | |
D | VAL1846 |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8605183, ECO:0000269|PubMed:9376357 |
Chain | Residue | Details |
A | ALA160 | |
B | THR897 | |
C | ALA1160 | |
C | PHE1169 | |
C | ASP1296 | |
C | ASP1321 | |
C | THR1397 | |
D | ALA1660 | |
D | PHE1669 | |
D | ASP1796 | |
D | ASP1821 | |
A | PHE169 | |
D | THR1897 | |
A | ASP296 | |
A | ASP321 | |
A | THR397 | |
B | ALA660 | |
B | PHE669 | |
B | ASP796 | |
B | ASP821 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8605183 |
Chain | Residue | Details |
A | CYS247 | |
B | CYS747 | |
C | CYS1247 | |
D | CYS1747 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12054465, ECO:0000269|PubMed:8605183, ECO:0000269|PubMed:9376357 |
Chain | Residue | Details |
A | HIS373 | |
B | HIS873 | |
C | HIS1373 | |
D | HIS1873 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358 |
Chain | Residue | Details |
A | ARG119 | |
B | ARG619 | |
C | ARG1119 | |
D | ARG1619 |
site_id | SWS_FT_FI7 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00925 |
Chain | Residue | Details |
A | LYS138 | |
A | GLU188 | |
B | LYS638 | |
B | GLU688 | |
C | LYS1138 | |
C | GLU1188 | |
D | LYS1638 | |
D | GLU1688 |
site_id | SWS_FT_FI8 |
Number of Residues | 8 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P00925 |
Chain | Residue | Details |
A | ALA313 | |
A | VAL324 | |
B | ALA813 | |
B | VAL824 | |
C | ALA1313 | |
C | VAL1324 | |
D | ALA1813 | |
D | VAL1824 |
site_id | SWS_FT_FI9 |
Number of Residues | 8 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P00925 |
Chain | Residue | Details |
A | GLY60 | |
A | ILE243 | |
B | GLY560 | |
B | ILE743 | |
C | GLY1060 | |
C | ILE1243 | |
D | GLY1560 | |
D | ILE1743 |
site_id | SWS_FT_FI10 |
Number of Residues | 8 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 |
Chain | Residue | Details |
A | ALA358 | |
B | ALA858 | |
C | ALA1358 | |
D | ALA1858 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 10 |
Details | M-CSA 311 |
Chain | Residue | Details |
A | THR40 | metal ligand |
A | THR397 | electrostatic stabiliser, hydrogen bond donor, proton shuttle (general acid/base) |
A | ALA160 | electrostatic stabiliser, proton shuttle (general acid/base) |
A | PHE169 | activator, electrostatic stabiliser, hydrogen bond acceptor, increase acidity, repulsive charge-charge interaction |
A | GLY212 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor |
A | CYS247 | metal ligand |
A | ASP296 | metal ligand |
A | ASP321 | metal ligand |
A | VAL346 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor |
A | ARG374 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 10 |
Details | M-CSA 311 |
Chain | Residue | Details |
B | THR540 | metal ligand |
B | THR897 | electrostatic stabiliser, hydrogen bond donor, proton shuttle (general acid/base) |
B | ALA660 | electrostatic stabiliser, proton shuttle (general acid/base) |
B | PHE669 | activator, electrostatic stabiliser, hydrogen bond acceptor, increase acidity, repulsive charge-charge interaction |
B | GLY712 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor |
B | CYS747 | metal ligand |
B | ASP796 | metal ligand |
B | ASP821 | metal ligand |
B | VAL846 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor |
B | ARG874 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA3 |
Number of Residues | 10 |
Details | M-CSA 311 |
Chain | Residue | Details |
C | THR1040 | metal ligand |
C | THR1397 | electrostatic stabiliser, hydrogen bond donor, proton shuttle (general acid/base) |
C | ALA1160 | electrostatic stabiliser, proton shuttle (general acid/base) |
C | PHE1169 | activator, electrostatic stabiliser, hydrogen bond acceptor, increase acidity, repulsive charge-charge interaction |
C | GLY1212 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor |
C | CYS1247 | metal ligand |
C | ASP1296 | metal ligand |
C | ASP1321 | metal ligand |
C | VAL1346 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor |
C | ARG1374 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA4 |
Number of Residues | 10 |
Details | M-CSA 311 |
Chain | Residue | Details |
D | THR1540 | metal ligand |
D | THR1897 | electrostatic stabiliser, hydrogen bond donor, proton shuttle (general acid/base) |
D | ALA1660 | electrostatic stabiliser, proton shuttle (general acid/base) |
D | PHE1669 | activator, electrostatic stabiliser, hydrogen bond acceptor, increase acidity, repulsive charge-charge interaction |
D | GLY1712 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor |
D | CYS1747 | metal ligand |
D | ASP1796 | metal ligand |
D | ASP1821 | metal ligand |
D | VAL1846 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor |
D | ARG1874 | electrostatic stabiliser, hydrogen bond donor |