2XH4
Engineering the enolase active site pocket: Crystal structure of the S39A D321A mutant of 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 | 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 |
| 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 | 0005515 | molecular_function | protein binding |
| 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 | 0005515 | molecular_function | protein binding |
| 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 1439 |
| Chain | Residue |
| A | ASP246 |
| A | GLU295 |
| A | ASP320 |
| A | 2PG1440 |
| A | HOH2402 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 2PG A 1440 |
| Chain | Residue |
| A | GLN167 |
| A | GLU168 |
| A | GLU211 |
| A | ASP246 |
| A | GLU295 |
| A | ASP320 |
| A | LYS345 |
| A | HIS373 |
| A | ARG374 |
| A | SER375 |
| A | LYS396 |
| A | MG1439 |
| A | HOH2098 |
| A | GLY37 |
| A | ALA38 |
| A | ALA39 |
| A | HIS159 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 1439 |
| Chain | Residue |
| B | ASP246 |
| B | GLU295 |
| B | ASP320 |
| B | 2PG1440 |
| B | HOH2275 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE 2PG B 1440 |
| Chain | Residue |
| B | GLY37 |
| B | HIS159 |
| B | GLN167 |
| B | GLU168 |
| B | GLU211 |
| B | ASP246 |
| B | GLU295 |
| B | ASP320 |
| B | LEU343 |
| B | LYS345 |
| B | HIS373 |
| B | ARG374 |
| B | SER375 |
| B | LYS396 |
| B | MG1439 |
| B | MG1441 |
| B | HOH2376 |
| B | HOH2377 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 1441 |
| Chain | Residue |
| B | LYS345 |
| B | 2PG1440 |
| B | HOH2186 |
| B | HOH2376 |
| B | HOH2377 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 1442 |
| Chain | Residue |
| B | GLU428 |
| B | HOH2079 |
| B | HOH2189 |
| B | HOH2364 |
| B | HOH2366 |
| B | HOH2368 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 1439 |
| Chain | Residue |
| C | ASP246 |
| C | GLU295 |
| C | ASP320 |
| C | 2PG1440 |
| C | HOH2381 |
| site_id | AC8 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 2PG C 1440 |
| Chain | Residue |
| C | GLY37 |
| C | ALA38 |
| C | ALA39 |
| C | HIS159 |
| C | GLN167 |
| C | GLU168 |
| C | GLU211 |
| C | ASP246 |
| C | GLU295 |
| C | ASP320 |
| C | LEU343 |
| C | LYS345 |
| C | HIS373 |
| C | ARG374 |
| C | SER375 |
| C | LYS396 |
| C | MG1439 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 1439 |
| Chain | Residue |
| D | ASP246 |
| D | GLU295 |
| D | ASP320 |
| D | 2PG1440 |
| D | HOH2211 |
| site_id | BC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE 2PG D 1440 |
| Chain | Residue |
| D | GLY37 |
| D | HIS159 |
| D | GLN167 |
| D | GLU168 |
| D | GLU211 |
| D | ASP246 |
| D | GLU295 |
| D | ASP320 |
| D | LEU343 |
| D | LYS345 |
| D | HIS373 |
| D | ARG374 |
| D | SER375 |
| D | LYS396 |
| D | MG1439 |
| D | HOH2312 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 1441 |
| Chain | Residue |
| D | GLU428 |
| D | HOH2072 |
| D | HOH2154 |
| D | HOH2299 |
| D | HOH2300 |
| D | HOH2301 |
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 | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"12846578","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| 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 | 20 |
| 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 | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8605183","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| 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 | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00925","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P00925","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 6 |
| 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 | 8 |
| 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 | MCSA1 |
| Number of Residues | 10 |
| Details | M-CSA 311 |
| Chain | Residue | Details |
| A | ALA39 | 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 |
| site_id | MCSA2 |
| Number of Residues | 9 |
| Details | M-CSA 311 |
| Chain | Residue | Details |
| B | HIS159 | electrostatic stabiliser, proton shuttle (general acid/base) |
| B | GLU168 | activator, electrostatic stabiliser, hydrogen bond acceptor, increase acidity, repulsive charge-charge interaction |
| B | GLU211 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor |
| B | ASP246 | metal ligand |
| B | GLU295 | metal ligand |
| B | ASP320 | metal ligand |
| B | LYS345 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor |
| B | HIS373 | electrostatic stabiliser, hydrogen bond donor |
| B | LYS396 | electrostatic stabiliser, hydrogen bond donor, proton shuttle (general acid/base) |
| site_id | MCSA3 |
| Number of Residues | 10 |
| Details | M-CSA 311 |
| Chain | Residue | Details |
| C | ALA39 | metal ligand |
| C | LYS396 | electrostatic stabiliser, hydrogen bond donor, proton shuttle (general acid/base) |
| C | HIS159 | electrostatic stabiliser, proton shuttle (general acid/base) |
| C | GLU168 | activator, electrostatic stabiliser, hydrogen bond acceptor, increase acidity, repulsive charge-charge interaction |
| C | GLU211 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor |
| C | ASP246 | metal ligand |
| C | GLU295 | metal ligand |
| C | ASP320 | metal ligand |
| C | LYS345 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor |
| C | HIS373 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA4 |
| Number of Residues | 9 |
| Details | M-CSA 311 |
| Chain | Residue | Details |
| D | HIS159 | electrostatic stabiliser, proton shuttle (general acid/base) |
| D | GLU168 | activator, electrostatic stabiliser, hydrogen bond acceptor, increase acidity, repulsive charge-charge interaction |
| D | GLU211 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor |
| D | ASP246 | metal ligand |
| D | GLU295 | metal ligand |
| D | ASP320 | metal ligand |
| D | LYS345 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor |
| D | HIS373 | electrostatic stabiliser, hydrogen bond donor |
| D | LYS396 | electrostatic stabiliser, hydrogen bond donor, proton shuttle (general acid/base) |
