4E4F
Crystal structure of enolase PC1_0802 (TARGET EFI-502240) from Pectobacterium carotovorum subsp. carotovorum PC1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0008927 | molecular_function | mannonate dehydratase activity |
| A | 0009063 | biological_process | amino acid catabolic process |
| A | 0016052 | biological_process | carbohydrate catabolic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0008927 | molecular_function | mannonate dehydratase activity |
| B | 0009063 | biological_process | amino acid catabolic process |
| B | 0016052 | biological_process | carbohydrate catabolic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0008927 | molecular_function | mannonate dehydratase activity |
| C | 0009063 | biological_process | amino acid catabolic process |
| C | 0016052 | biological_process | carbohydrate catabolic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0008927 | molecular_function | mannonate dehydratase activity |
| D | 0009063 | biological_process | amino acid catabolic process |
| D | 0016052 | biological_process | carbohydrate catabolic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 501 |
| Chain | Residue |
| A | ASN37 |
| A | PRO171 |
| A | HIS314 |
| A | PRO316 |
| A | ASP318 |
| A | LEU391 |
| A | FMT506 |
| D | TRP76 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 502 |
| Chain | Residue |
| A | VAL81 |
| D | PRO80 |
| D | VAL81 |
| A | PRO80 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 503 |
| Chain | Residue |
| A | PRO242 |
| A | ALA243 |
| A | GLU244 |
| A | ASN245 |
| A | HOH743 |
| B | SER305 |
| B | GLN308 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 504 |
| Chain | Residue |
| A | ASP212 |
| A | GLU238 |
| A | ASP239 |
| A | GLU264 |
| A | FMT506 |
| A | HOH762 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 505 |
| Chain | Residue |
| A | THR218 |
| A | PRO242 |
| A | TRP402 |
| A | ASN403 |
| A | HOH801 |
| B | GLN308 |
| D | LYS72 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FMT A 506 |
| Chain | Residue |
| A | ASP212 |
| A | GLU238 |
| A | GLU264 |
| A | ARG285 |
| A | GOL501 |
| A | MG504 |
| A | HOH649 |
| A | HOH762 |
| D | TYR75 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 501 |
| Chain | Residue |
| B | ASN37 |
| B | HIS314 |
| B | PRO316 |
| B | ASP318 |
| B | FMT506 |
| C | TRP76 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 502 |
| Chain | Residue |
| A | LEU306 |
| A | GLN308 |
| B | PRO242 |
| B | ALA243 |
| B | GLU244 |
| B | ASN245 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 503 |
| Chain | Residue |
| B | PRO80 |
| B | VAL81 |
| C | PRO80 |
| C | VAL81 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 504 |
| Chain | Residue |
| A | GLN308 |
| B | THR218 |
| B | PRO242 |
| B | TRP402 |
| B | ASN403 |
| C | LYS72 |
| C | HOH618 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 505 |
| Chain | Residue |
| B | ASP212 |
| B | GLU238 |
| B | ASP239 |
| B | GLU264 |
| B | FMT506 |
| B | HOH769 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT B 506 |
| Chain | Residue |
| B | ASP212 |
| B | GLU238 |
| B | GLU264 |
| B | ARG285 |
| B | GOL501 |
| B | MG505 |
| B | HOH751 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 501 |
| Chain | Residue |
| B | TRP76 |
| C | ASN37 |
| C | HIS314 |
| C | PRO316 |
| C | ASP318 |
| C | FMT505 |
| C | HOH692 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 502 |
| Chain | Residue |
| B | TRP270 |
| C | GLU244 |
| C | ASN245 |
| C | GLN246 |
| C | ALA247 |
| C | GLN274 |
| C | HOH750 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 503 |
| Chain | Residue |
| B | LYS72 |
| B | HOH735 |
| C | PRO242 |
| C | TRP402 |
| C | ASN403 |
| C | HOH773 |
| D | GLN308 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 504 |
| Chain | Residue |
| C | GLU238 |
| C | GLU264 |
| C | FMT505 |
| C | HOH761 |
| C | ASP212 |
| site_id | BC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FMT C 505 |
| Chain | Residue |
| C | ASP212 |
| C | GLU238 |
| C | GLU264 |
| C | ARG285 |
| C | GOL501 |
| C | MG504 |
| C | HOH643 |
| C | HOH692 |
| site_id | BC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 501 |
| Chain | Residue |
| A | TRP76 |
| D | ASN37 |
| D | PRO171 |
| D | HIS314 |
| D | PRO316 |
| D | ASP318 |
| D | TRP404 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 502 |
| Chain | Residue |
| A | HOH767 |
| D | TYR71 |
| D | SER268 |
| D | ILE269 |
| D | GLY296 |
| D | ARG299 |
| site_id | CC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 503 |
| Chain | Residue |
| D | ASP212 |
| D | GLU238 |
| D | ASP239 |
| D | GLU264 |
| D | FMT505 |
| D | HOH741 |
| site_id | CC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL D 504 |
| Chain | Residue |
| A | TRP270 |
| C | SER305 |
| C | LEU306 |
| C | GLN308 |
| D | PRO242 |
| D | ALA243 |
| D | GLU244 |
| D | ASN245 |
| site_id | CC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FMT D 505 |
| Chain | Residue |
| A | TYR75 |
| D | ASP212 |
| D | HIS214 |
| D | GLU238 |
| D | GLU264 |
| D | ARG285 |
| D | MG503 |
| D | HOH663 |
| D | HOH741 |
Functional Information from PROSITE/UniProt
| site_id | PS00908 |
| Number of Residues | 26 |
| Details | MR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. AiSAVDmALwDIkAKaanmPLyqLLG |
| Chain | Residue | Details |
| A | ALA85-GLY110 |
| site_id | PS00909 |
| Number of Residues | 32 |
| Details | MR_MLE_2 Mandelate racemase / muconate lactonizing enzyme family signature 2. LlhDmHhrltpieAarfgksVedyrlfwMEDP |
| Chain | Residue | Details |
| A | LEU209-PRO240 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000250 |
| Chain | Residue | Details |
| A | TYR159 | |
| A | HIS214 | |
| B | TYR159 | |
| B | HIS214 | |
| C | TYR159 | |
| C | HIS214 | |
| D | TYR159 | |
| D | HIS214 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ASN37 | |
| B | GLU264 | |
| B | ARG285 | |
| B | HIS314 | |
| B | ASP318 | |
| B | GLU341 | |
| C | ASN37 | |
| C | HIS122 | |
| C | GLU264 | |
| C | ARG285 | |
| C | HIS314 | |
| A | HIS122 | |
| C | ASP318 | |
| C | GLU341 | |
| D | ASN37 | |
| D | HIS122 | |
| D | GLU264 | |
| D | ARG285 | |
| D | HIS314 | |
| D | ASP318 | |
| D | GLU341 | |
| A | GLU264 | |
| A | ARG285 | |
| A | HIS314 | |
| A | ASP318 | |
| A | GLU341 | |
| B | ASN37 | |
| B | HIS122 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24697546 |
| Chain | Residue | Details |
| A | ASP212 | |
| A | GLU238 | |
| B | ASP212 | |
| B | GLU238 | |
| C | ASP212 | |
| C | GLU238 | |
| D | ASP212 | |
| D | GLU238 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | SITE: Important for activity and substrate specificity; Pro is observed in family members with low D-mannonate dehydratase activity => ECO:0000250 |
| Chain | Residue | Details |
| A | PRO316 | |
| B | PRO316 | |
| C | PRO316 | |
| D | PRO316 |
