1EC9
E. COLI GLUCARATE DEHYDRATASE BOUND TO XYLAROHYDROXAMATE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0008872 | molecular_function | glucarate dehydratase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019394 | biological_process | glucarate catabolic process |
| A | 0042838 | biological_process | D-glucarate catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0008872 | molecular_function | glucarate dehydratase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019394 | biological_process | glucarate catabolic process |
| B | 0042838 | biological_process | D-glucarate catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0008872 | molecular_function | glucarate dehydratase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0019394 | biological_process | glucarate catabolic process |
| C | 0042838 | biological_process | D-glucarate catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0008872 | molecular_function | glucarate dehydratase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0019394 | biological_process | glucarate catabolic process |
| D | 0042838 | biological_process | D-glucarate catabolic process |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 498 |
| Chain | Residue |
| A | ASP235 |
| A | GLU260 |
| A | ASN289 |
| A | XYH499 |
| A | HOH1760 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 498 |
| Chain | Residue |
| B | XYH500 |
| B | HOH1755 |
| B | LYS207 |
| B | ASP235 |
| B | GLU260 |
| B | ASN289 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 498 |
| Chain | Residue |
| C | LYS205 |
| C | ASP235 |
| C | GLU260 |
| C | ASN289 |
| C | XYH501 |
| C | HOH1856 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 498 |
| Chain | Residue |
| D | LYS205 |
| D | ASP235 |
| D | GLU260 |
| D | ASN289 |
| D | XYH502 |
| D | HOH1757 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE XYH A 499 |
| Chain | Residue |
| A | ASN27 |
| A | HIS32 |
| A | THR103 |
| A | TYR150 |
| A | PHE152 |
| A | LYS205 |
| A | LYS207 |
| A | ASP235 |
| A | ASN237 |
| A | GLU260 |
| A | ASN289 |
| A | HIS339 |
| A | SER340 |
| A | ASN341 |
| A | HIS368 |
| A | ARG422 |
| A | MG498 |
| A | HOH1044 |
| A | HOH1760 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE XYH B 500 |
| Chain | Residue |
| B | ASN27 |
| B | HIS32 |
| B | THR103 |
| B | PHE104 |
| B | TYR150 |
| B | PHE152 |
| B | LYS205 |
| B | LYS207 |
| B | ASP235 |
| B | ASN237 |
| B | GLU260 |
| B | ASN289 |
| B | HIS339 |
| B | SER340 |
| B | ASN341 |
| B | HIS368 |
| B | ARG422 |
| B | MG498 |
| B | HOH1173 |
| B | HOH1755 |
| B | HOH1758 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE XYH C 501 |
| Chain | Residue |
| C | ASN27 |
| C | HIS32 |
| C | THR103 |
| C | TYR150 |
| C | PHE152 |
| C | LYS205 |
| C | LYS207 |
| C | ASP235 |
| C | ASN237 |
| C | GLU260 |
| C | ASN289 |
| C | HIS339 |
| C | SER340 |
| C | ASN341 |
| C | HIS368 |
| C | ARG422 |
| C | MG498 |
| C | HOH1154 |
| C | HOH1564 |
| C | HOH1856 |
| site_id | AC8 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE XYH D 502 |
| Chain | Residue |
| D | MG498 |
| D | HOH1066 |
| D | HOH1479 |
| D | HOH1757 |
| D | ASN27 |
| D | HIS32 |
| D | THR103 |
| D | TYR150 |
| D | PHE152 |
| D | LYS205 |
| D | LYS207 |
| D | ASP235 |
| D | ASN237 |
| D | GLU260 |
| D | ASN289 |
| D | HIS339 |
| D | SER340 |
| D | ASN341 |
| D | HIS368 |
| D | ARG422 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE IPA A 601 |
| Chain | Residue |
| A | GLY299 |
| A | SER303 |
| C | LEU302 |
| C | PHE332 |
| C | HOH1399 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE IPA D 602 |
| Chain | Residue |
| B | GLY299 |
| B | SER303 |
| D | LEU302 |
| D | PHE332 |
| D | HOH1314 |
| D | HOH1473 |
| D | HOH1793 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE IPA A 603 |
| Chain | Residue |
| A | LEU302 |
| A | PHE332 |
| A | HOH1871 |
| C | GLY299 |
| C | LEU302 |
| C | SER303 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE IPA B 604 |
| Chain | Residue |
| B | LEU302 |
| B | PHE332 |
| B | HOH1637 |
| D | GLY299 |
| D | SER303 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"11513584","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 44 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11513584","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 11513584, 10769114 |
| Chain | Residue | Details |
| A | HIS339 | |
| A | LYS207 | |
| A | LYS205 | |
| A | ASN237 |
| site_id | MCSA1 |
| Number of Residues | 9 |
| Details | M-CSA 451 |
| Chain | Residue | Details |
| A | LYS205 | electrostatic stabiliser |
| A | LYS207 | electrostatic stabiliser |
| A | ASP235 | metal ligand |
| A | ASN237 | activator, electrostatic stabiliser |
| A | GLU260 | metal ligand |
| A | ASN289 | metal ligand |
| A | ASP313 | electrostatic stabiliser, modifies pKa |
| A | HIS339 | proton acceptor, proton donor |
| A | ASN341 | activator |
| site_id | MCSA2 |
| Number of Residues | 9 |
| Details | M-CSA 451 |
| Chain | Residue | Details |
| B | LYS205 | electrostatic stabiliser |
| B | LYS207 | electrostatic stabiliser |
| B | ASP235 | metal ligand |
| B | ASN237 | activator, electrostatic stabiliser |
| B | GLU260 | metal ligand |
| B | ASN289 | metal ligand |
| B | ASP313 | electrostatic stabiliser, modifies pKa |
| B | HIS339 | proton acceptor, proton donor |
| B | ASN341 | activator |
| site_id | MCSA3 |
| Number of Residues | 9 |
| Details | M-CSA 451 |
| Chain | Residue | Details |
| C | LYS205 | electrostatic stabiliser |
| C | LYS207 | electrostatic stabiliser |
| C | ASP235 | metal ligand |
| C | ASN237 | activator, electrostatic stabiliser |
| C | GLU260 | metal ligand |
| C | ASN289 | metal ligand |
| C | ASP313 | electrostatic stabiliser, modifies pKa |
| C | HIS339 | proton acceptor, proton donor |
| C | ASN341 | activator |
| site_id | MCSA4 |
| Number of Residues | 9 |
| Details | M-CSA 451 |
| Chain | Residue | Details |
| D | LYS205 | electrostatic stabiliser |
| D | LYS207 | electrostatic stabiliser |
| D | ASP235 | metal ligand |
| D | ASN237 | activator, electrostatic stabiliser |
| D | GLU260 | metal ligand |
| D | ASN289 | metal ligand |
| D | ASP313 | electrostatic stabiliser, modifies pKa |
| D | HIS339 | proton acceptor, proton donor |
| D | ASN341 | activator |
