4GYP
Crystal structure of the heterotetrameric complex of GlucD and GlucDRP from E. coli K-12 MG1655 (EFI TARGET EFI-506058)
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 | 0008872 | molecular_function | glucarate dehydratase activity |
| C | 0009063 | biological_process | amino acid catabolic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0042838 | biological_process | D-glucarate catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0008872 | molecular_function | glucarate dehydratase activity |
| D | 0009063 | biological_process | amino acid catabolic process |
| D | 0016829 | molecular_function | lyase activity |
| 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 501 |
| Chain | Residue |
| A | ASP235 |
| A | ASN237 |
| A | GLU260 |
| A | ASP261 |
| A | ASN289 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 502 |
| Chain | Residue |
| A | ASN341 |
| A | HIS368 |
| A | ARG422 |
| A | HOH601 |
| A | HOH610 |
| A | HOH613 |
| A | ASN27 |
| A | HIS32 |
| A | PHE152 |
| A | LYS207 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 503 |
| Chain | Residue |
| A | GLY299 |
| A | SER303 |
| A | HOH832 |
| A | HOH995 |
| B | LEU302 |
| B | GLN305 |
| B | PHE332 |
| D | ARG279 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PEG A 504 |
| Chain | Residue |
| A | HIS49 |
| A | GLN126 |
| A | HIS127 |
| A | GLY129 |
| A | HOH617 |
| A | HOH719 |
| A | HOH924 |
| B | PHE5 |
| D | GLY169 |
| D | ASN170 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 501 |
| Chain | Residue |
| B | ASP235 |
| B | ASN237 |
| B | GLU260 |
| B | ASP261 |
| B | ASN289 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 B 502 |
| Chain | Residue |
| B | ASN27 |
| B | HIS32 |
| B | PHE152 |
| B | LYS207 |
| B | ASN341 |
| B | HIS368 |
| B | ARG422 |
| B | HOH604 |
| B | HOH672 |
| B | HOH678 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE CIT C 501 |
| Chain | Residue |
| C | ASN26 |
| C | ILE27 |
| C | HIS31 |
| C | LYS206 |
| C | ASN236 |
| C | HIS338 |
| C | ASN340 |
| C | HIS367 |
| C | ARG421 |
| C | HOH667 |
| C | HOH728 |
| C | HOH874 |
| C | HOH910 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 502 |
| Chain | Residue |
| A | LEU302 |
| A | PHE332 |
| A | HOH995 |
| B | GLY299 |
| B | SER303 |
| C | ARG279 |
| C | HOH680 |
| C | HOH814 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG C 503 |
| Chain | Residue |
| C | ASN80 |
| C | HOH940 |
| D | ASN80 |
| D | LEU123 |
| site_id | BC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CIT D 501 |
| Chain | Residue |
| D | ASN26 |
| D | ILE27 |
| D | HIS31 |
| D | TRP103 |
| D | PHE105 |
| D | PHE151 |
| D | LYS206 |
| D | ASN236 |
| D | HIS338 |
| D | ASN340 |
| D | HIS367 |
| D | ARG421 |
| D | HOH629 |
| D | HOH694 |
| D | HOH733 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE P6G D 502 |
| Chain | Residue |
| B | GLY283 |
| B | PRO285 |
| B | ASP308 |
| D | ARG279 |
| D | GLY282 |
| D | PRO284 |
| D | ASP307 |
| D | HOH604 |
| D | HOH758 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 503 |
| Chain | Residue |
| D | SER319 |
| D | ARG323 |
| D | HOH606 |
| D | HOH639 |
| C | HOH685 |
| D | THR317 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 504 |
| Chain | Residue |
| A | GLN391 |
| A | HOH731 |
| A | HOH925 |
| A | HOH926 |
| D | ARG376 |
| D | ASP402 |
| D | GLU404 |
| D | GLN405 |
| D | LYS408 |
| site_id | BC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PEG D 505 |
| Chain | Residue |
| D | ASN360 |
Functional Information from PROSITE/UniProt
| site_id | PS00908 |
| Number of Residues | 26 |
| Details | MR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. AvAALEaALlDLlGKalnvPVceLLG |
| Chain | Residue | Details |
| C | ALA111-GLY136 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| 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 | 22 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11513584","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 21 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| 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 |
