1EBH
OCTAHEDRAL COORDINATION AT THE HIGH AFFINITY METAL SITE IN ENOLASE; CRYSTALLOGRAPHIC ANALYSIS OF THE MG++-ENZYME FROM YEAST AT 1.9 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 | 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 437 |
| Chain | Residue |
| A | ARG374 |
| A | SER375 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 438 |
| Chain | Residue |
| A | ASP246 |
| A | GLU295 |
| A | ASP320 |
| A | HOH439 |
| A | HOH440 |
| A | HOH441 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 437 |
| Chain | Residue |
| B | GLY37 |
| B | ARG374 |
| B | SER375 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 438 |
| Chain | Residue |
| B | ASP246 |
| B | GLU295 |
| B | ASP320 |
| B | HOH439 |
| B | HOH440 |
| B | HOH441 |
| site_id | MIA |
| Number of Residues | 6 |
| Details | METAL BINDING SITE |
| Chain | Residue |
| A | ASP246 |
| A | GLU295 |
| A | ASP320 |
| A | ALA1 |
| A | VAL2 |
| A | SER3 |
| site_id | MIB |
| Number of Residues | 6 |
| Details | METAL BINDING SITE |
| Chain | Residue |
| B | GLU295 |
| B | ASP320 |
| B | ALA1 |
| B | VAL2 |
| B | SER3 |
| B | ASP246 |
| site_id | PHA |
| Number of Residues | 2 |
| Details | PHOSPHATE BINDING SITE |
| Chain | Residue |
| A | SER375 |
| A | ARG374 |
| site_id | PHB |
| Number of Residues | 2 |
| Details | PHOSPHATE BINDING SITE |
| Chain | Residue |
| B | SER375 |
| B | ARG374 |
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 | ACT_SITE: Proton donor => ECO:0000269|PubMed:12846578 |
| Chain | Residue | Details |
| A | GLY212 | |
| B | GLY212 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:12846578, ECO:0000269|PubMed:8634301 |
| Chain | Residue | Details |
| A | VAL346 | |
| B | VAL346 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8605183, ECO:0000269|PubMed:9376357 |
| Chain | Residue | Details |
| B | PHE169 | |
| B | ASP296 | |
| B | ASP321 | |
| B | THR397 | |
| A | ALA160 | |
| A | PHE169 | |
| A | ASP296 | |
| A | ASP321 | |
| A | THR397 | |
| B | ALA160 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8605183 |
| Chain | Residue | Details |
| A | CYS247 | |
| B | CYS247 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12054465, ECO:0000269|PubMed:8605183, ECO:0000269|PubMed:9376357 |
| Chain | Residue | Details |
| A | HIS373 | |
| B | HIS373 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358 |
| Chain | Residue | Details |
| A | ARG119 | |
| B | ARG119 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00925 |
| Chain | Residue | Details |
| A | LYS138 | |
| A | GLU188 | |
| B | LYS138 | |
| B | GLU188 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P00925 |
| Chain | Residue | Details |
| A | ALA313 | |
| A | VAL324 | |
| B | ALA313 | |
| B | VAL324 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P00925 |
| Chain | Residue | Details |
| A | GLY60 | |
| B | GLY60 | |
| A | ILE243 | |
| B | ILE243 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 |
| Chain | Residue | Details |
| A | ALA358 | |
| B | ALA358 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 10 |
| Details | M-CSA 311 |
| Chain | Residue | Details |
| A | THR40 | metal ligand |
| 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 |
| A | THR397 | electrostatic stabiliser, hydrogen bond donor, proton shuttle (general acid/base) |
| site_id | MCSA2 |
| Number of Residues | 10 |
| Details | M-CSA 311 |
| Chain | Residue | Details |
| B | THR40 | metal ligand |
| B | ALA160 | electrostatic stabiliser, proton shuttle (general acid/base) |
| B | PHE169 | activator, electrostatic stabiliser, hydrogen bond acceptor, increase acidity, repulsive charge-charge interaction |
| B | GLY212 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor |
| B | CYS247 | metal ligand |
| B | ASP296 | metal ligand |
| B | ASP321 | metal ligand |
| B | VAL346 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor |
| B | ARG374 | electrostatic stabiliser, hydrogen bond donor |
| B | THR397 | electrostatic stabiliser, hydrogen bond donor, proton shuttle (general acid/base) |
