4IL0
Crystal structure of GlucDRP from E. coli K-12 MG1655 (EFI target EFI-506058)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0009063 | biological_process | amino acid catabolic process |
A | 0016829 | molecular_function | lyase activity |
A | 0044248 | biological_process | cellular catabolic process |
A | 0046872 | molecular_function | metal ion binding |
B | 0009063 | biological_process | amino acid catabolic process |
B | 0016829 | molecular_function | lyase activity |
B | 0044248 | biological_process | cellular catabolic process |
B | 0046872 | molecular_function | metal ion binding |
C | 0009063 | biological_process | amino acid catabolic process |
C | 0016829 | molecular_function | lyase activity |
C | 0044248 | biological_process | cellular catabolic process |
C | 0046872 | molecular_function | metal ion binding |
D | 0009063 | biological_process | amino acid catabolic process |
D | 0016829 | molecular_function | lyase activity |
D | 0044248 | biological_process | cellular catabolic process |
D | 0046872 | molecular_function | metal ion binding |
E | 0009063 | biological_process | amino acid catabolic process |
E | 0016829 | molecular_function | lyase activity |
E | 0044248 | biological_process | cellular catabolic process |
E | 0046872 | molecular_function | metal ion binding |
F | 0009063 | biological_process | amino acid catabolic process |
F | 0016829 | molecular_function | lyase activity |
F | 0044248 | biological_process | cellular catabolic process |
F | 0046872 | molecular_function | metal ion binding |
G | 0009063 | biological_process | amino acid catabolic process |
G | 0016829 | molecular_function | lyase activity |
G | 0044248 | biological_process | cellular catabolic process |
G | 0046872 | molecular_function | metal ion binding |
H | 0009063 | biological_process | amino acid catabolic process |
H | 0016829 | molecular_function | lyase activity |
H | 0044248 | biological_process | cellular catabolic process |
H | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE CIT A 501 |
Chain | Residue |
A | ASN26 |
A | HIS367 |
A | ARG421 |
A | ILE27 |
A | HIS31 |
A | TRP103 |
A | PHE105 |
A | LYS206 |
A | ASN236 |
A | HIS338 |
A | ASN340 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE CIT B 501 |
Chain | Residue |
B | ASN26 |
B | HIS31 |
B | TRP103 |
B | PHE105 |
B | PHE151 |
B | LYS206 |
B | ASN236 |
B | HIS338 |
B | ASN340 |
B | HIS367 |
B | ARG421 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE CIT C 501 |
Chain | Residue |
C | ASN26 |
C | ILE27 |
C | HIS31 |
C | TRP103 |
C | PHE105 |
C | LYS206 |
C | ASN236 |
C | HIS338 |
C | ASN340 |
C | HIS367 |
C | ARG421 |
site_id | AC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE CIT D 501 |
Chain | Residue |
D | ASN26 |
D | ILE27 |
D | HIS31 |
D | PHE105 |
D | PHE151 |
D | LYS206 |
D | ASN236 |
D | HIS338 |
D | ASN340 |
D | HIS367 |
D | ARG421 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CIT E 501 |
Chain | Residue |
E | ASN26 |
E | HIS31 |
E | LYS206 |
E | ASN236 |
E | HIS338 |
E | ASN340 |
E | HIS367 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL E 502 |
Chain | Residue |
E | GLY169 |
E | ASN170 |
E | HIS171 |
site_id | AC7 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE CIT F 501 |
Chain | Residue |
F | ASN26 |
F | ILE27 |
F | HIS31 |
F | TRP103 |
F | PHE105 |
F | PHE151 |
F | LYS206 |
F | ASN236 |
F | HIS338 |
F | ASN340 |
F | HIS367 |
F | ARG421 |
site_id | AC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE CIT G 501 |
Chain | Residue |
G | ASN26 |
G | ILE27 |
G | HIS31 |
G | PHE151 |
G | LYS206 |
G | ASN236 |
G | HIS338 |
G | ASN340 |
G | HIS367 |
G | ARG421 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL G 502 |
Chain | Residue |
G | ASN170 |
G | HIS171 |
site_id | BC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE CIT H 501 |
Chain | Residue |
H | ASN26 |
H | ILE27 |
H | HIS31 |
H | TRP103 |
H | PHE105 |
H | PHE151 |
H | LYS206 |
H | ASN236 |
H | HIS338 |
H | ASN340 |
H | HIS367 |
H | ARG421 |
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 |
A | ALA111-GLY136 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | ACT_SITE: Proton acceptor => ECO:0000255 |
Chain | Residue | Details |
A | LYS206 | |
E | HIS338 | |
F | LYS206 | |
F | HIS338 | |
G | LYS206 | |
G | HIS338 | |
H | LYS206 | |
H | HIS338 | |
A | HIS338 | |
B | LYS206 | |
B | HIS338 | |
C | LYS206 | |
C | HIS338 | |
D | LYS206 | |
D | HIS338 | |
E | LYS206 |
site_id | SWS_FT_FI2 |
Number of Residues | 64 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | HIS31 | |
B | THR104 | |
B | TYR149 | |
B | LYS204 | |
B | ASN288 | |
B | HIS338 | |
B | HIS367 | |
B | ARG421 | |
C | HIS31 | |
C | THR104 | |
C | TYR149 | |
A | THR104 | |
C | LYS204 | |
C | ASN288 | |
C | HIS338 | |
C | HIS367 | |
C | ARG421 | |
D | HIS31 | |
D | THR104 | |
D | TYR149 | |
D | LYS204 | |
D | ASN288 | |
A | TYR149 | |
D | HIS338 | |
D | HIS367 | |
D | ARG421 | |
E | HIS31 | |
E | THR104 | |
E | TYR149 | |
E | LYS204 | |
E | ASN288 | |
E | HIS338 | |
E | HIS367 | |
A | LYS204 | |
E | ARG421 | |
F | HIS31 | |
F | THR104 | |
F | TYR149 | |
F | LYS204 | |
F | ASN288 | |
F | HIS338 | |
F | HIS367 | |
F | ARG421 | |
G | HIS31 | |
A | ASN288 | |
G | THR104 | |
G | TYR149 | |
G | LYS204 | |
G | ASN288 | |
G | HIS338 | |
G | HIS367 | |
G | ARG421 | |
H | HIS31 | |
H | THR104 | |
H | TYR149 | |
A | HIS338 | |
H | LYS204 | |
H | ASN288 | |
H | HIS338 | |
H | HIS367 | |
H | ARG421 | |
A | HIS367 | |
A | ARG421 | |
B | HIS31 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000255 |
Chain | Residue | Details |
A | ASP234 | |
E | GLU265 | |
F | ASP234 | |
F | GLU265 | |
G | ASP234 | |
G | GLU265 | |
H | ASP234 | |
H | GLU265 | |
A | GLU265 | |
B | ASP234 | |
B | GLU265 | |
C | ASP234 | |
C | GLU265 | |
D | ASP234 | |
D | GLU265 | |
E | ASP234 |