2XGZ
Engineering the enolase active site pocket: Crystal structure of the S39N D321R 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 | 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 | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 1439 |
| Chain | Residue |
| A | ASP246 |
| A | GLU295 |
| A | ASP320 |
| A | LYS396 |
| A | PEP1440 |
| A | HOH2298 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PEP A 1440 |
| Chain | Residue |
| A | GLU211 |
| A | ASP246 |
| A | GLU295 |
| A | ASP320 |
| A | ARG321 |
| A | LEU343 |
| A | LYS345 |
| A | ARG374 |
| A | SER375 |
| A | LYS396 |
| A | MG1439 |
| A | HOH2233 |
| A | HOH2407 |
| A | GLY37 |
| A | ALA38 |
| A | GLU168 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 1441 |
| Chain | Residue |
| A | ASP135 |
| A | HOH2195 |
| A | HOH2201 |
| A | HOH2202 |
| A | HOH2213 |
| B | HOH2272 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 1442 |
| Chain | Residue |
| A | HOH2062 |
| A | HOH2109 |
| A | HOH2110 |
| A | HOH2163 |
| B | HOH2298 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 1439 |
| Chain | Residue |
| B | ASP246 |
| B | GLU295 |
| B | ASP320 |
| B | PEP1440 |
| B | HOH2293 |
| B | HOH2392 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PEP B 1440 |
| Chain | Residue |
| B | GLN167 |
| B | GLU168 |
| B | ASP246 |
| B | GLU295 |
| B | ASP320 |
| B | LYS345 |
| B | SER372 |
| B | SER375 |
| B | LYS396 |
| B | MG1439 |
| B | HOH2392 |
| B | HOH2393 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 1441 |
| Chain | Residue |
| A | HOH2263 |
| B | ASP135 |
| B | HOH2090 |
| B | HOH2193 |
| B | HOH2194 |
| B | HOH2208 |
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 | GLU211 | |
| B | GLU211 |
| 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 | LYS345 | |
| B | LYS345 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8605183, ECO:0000269|PubMed:9376357 |
| Chain | Residue | Details |
| A | HIS159 | |
| B | LYS396 | |
| A | GLU168 | |
| A | GLU295 | |
| A | ASP320 | |
| A | LYS396 | |
| B | HIS159 | |
| B | GLU168 | |
| B | GLU295 | |
| B | ASP320 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8605183 |
| Chain | Residue | Details |
| A | ASP246 | |
| B | ASP246 |
| 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 | SER372 | |
| B | SER372 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358 |
| Chain | Residue | Details |
| A | SER118 | |
| B | SER118 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00925 |
| Chain | Residue | Details |
| A | SER137 | |
| A | SER187 | |
| B | SER137 | |
| B | SER187 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P00925 |
| Chain | Residue | Details |
| A | THR312 | |
| A | THR323 | |
| B | THR312 | |
| B | THR323 |
| 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 | LYS59 | |
| A | LYS242 | |
| B | LYS59 | |
| B | LYS242 |
| 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 | LYS357 | |
| B | LYS357 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 10 |
| Details | M-CSA 311 |
| Chain | Residue | Details |
| A | ASN39 | 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 | 10 |
| Details | M-CSA 311 |
| Chain | Residue | Details |
| B | ASN39 | metal ligand |
| B | LYS396 | electrostatic stabiliser, hydrogen bond donor, proton shuttle (general acid/base) |
| 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 |
