3CT2
Crystal structure of muconate cycloisomerase from Pseudomonas fluorescens
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006518 | biological_process | peptide metabolic process |
A | 0009063 | biological_process | amino acid catabolic process |
A | 0016853 | molecular_function | isomerase activity |
A | 0016854 | molecular_function | racemase and epimerase activity |
A | 0018849 | molecular_function | muconate cycloisomerase activity |
A | 0018850 | molecular_function | chloromuconate cycloisomerase activity |
A | 0030145 | molecular_function | manganese ion binding |
A | 0046872 | molecular_function | metal ion binding |
B | 0006518 | biological_process | peptide metabolic process |
B | 0009063 | biological_process | amino acid catabolic process |
B | 0016853 | molecular_function | isomerase activity |
B | 0016854 | molecular_function | racemase and epimerase activity |
B | 0018849 | molecular_function | muconate cycloisomerase activity |
B | 0018850 | molecular_function | chloromuconate cycloisomerase activity |
B | 0030145 | molecular_function | manganese ion binding |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG A 401 |
Chain | Residue |
A | ASP200 |
A | GLU226 |
A | ASP251 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG B 401 |
Chain | Residue |
B | ASP200 |
B | GLU226 |
B | ASP251 |
Functional Information from PROSITE/UniProt
site_id | PS00908 |
Number of Residues | 26 |
Details | MR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. AkSGIEsALlDAqGKrlglPVseLLG |
Chain | Residue | Details |
A | ALA106-GLY131 |
site_id | PS00909 |
Number of Residues | 32 |
Details | MR_MLE_2 Mandelate racemase / muconate lactonizing enzyme family signature 2. VrvDvNqawdeavAlracriLggngidlIEQP |
Chain | Residue | Details |
A | VAL197-PRO228 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1muc |
Chain | Residue | Details |
A | GLU329 | |
A | LYS169 | |
A | LYS171 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1muc |
Chain | Residue | Details |
B | GLU329 | |
B | LYS169 | |
B | LYS171 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1muc |
Chain | Residue | Details |
A | LYS275 | |
A | LYS171 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1muc |
Chain | Residue | Details |
B | LYS275 | |
B | LYS171 |
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 269 |
Chain | Residue | Details |
A | LYS169 | electrostatic stabiliser |
A | LYS171 | electrostatic stabiliser, proton donor |
A | ASP200 | metal ligand |
A | GLU226 | metal ligand |
A | ASP251 | metal ligand |
A | LYS275 | electrostatic stabiliser |
A | GLU329 | proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 7 |
Details | M-CSA 269 |
Chain | Residue | Details |
B | LYS169 | electrostatic stabiliser |
B | LYS171 | electrostatic stabiliser, proton donor |
B | ASP200 | metal ligand |
B | GLU226 | metal ligand |
B | ASP251 | metal ligand |
B | LYS275 | electrostatic stabiliser |
B | GLU329 | proton acceptor, proton donor |