Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0006508 | biological_process | proteolysis |
A | 0008233 | molecular_function | peptidase activity |
A | 0036524 | molecular_function | protein deglycase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006508 | biological_process | proteolysis |
B | 0008233 | molecular_function | peptidase activity |
B | 0036524 | molecular_function | protein deglycase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0006508 | biological_process | proteolysis |
C | 0008233 | molecular_function | peptidase activity |
C | 0036524 | molecular_function | protein deglycase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue 7MT A 201 |
Chain | Residue |
A | ALA8 |
A | ASN9 |
A | PHE35 |
A | GLU36 |
A | ARG75 |
A | MLI202 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue MLI A 202 |
Chain | Residue |
A | ASN9 |
A | ARG75 |
A | 7MT201 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue TB A 204 |
Chain | Residue |
A | GLU10 |
A | HOH456 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue 7MT B 201 |
Chain | Residue |
B | ALA8 |
B | ASN9 |
B | PHE35 |
B | GLU36 |
B | ARG75 |
B | MLI202 |
B | HOH386 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue MLI B 202 |
Chain | Residue |
B | ASN9 |
B | ARG75 |
B | 7MT201 |
B | HOH386 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue TB B 203 |
Chain | Residue |
B | HOH397 |
B | HOH450 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue 7MT C 201 |
Chain | Residue |
C | ALA8 |
C | ASN9 |
C | PHE35 |
C | GLU36 |
C | ARG75 |
C | MLI202 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue MLI C 202 |
Chain | Residue |
C | ASN9 |
C | ARG75 |
C | 7MT201 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue TB C 203 |
Chain | Residue |
B | HOH417 |
C | HOH364 |
C | HOH373 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | CYS100 | |
B | CYS100 | |
C | CYS100 | |
Chain | Residue | Details |
A | HIS101 | |
B | HIS101 | |
C | HIS101 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 964 |
Chain | Residue | Details |
A | GLY70 | electrostatic stabiliser |
A | ARG71 | electrostatic stabiliser |
A | GLU74 | electrostatic stabiliser, modifies pKa |
A | CYS100 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
A | HIS101 | electrostatic stabiliser, proton acceptor, proton donor |
A | TYR120 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 964 |
Chain | Residue | Details |
B | GLY70 | electrostatic stabiliser |
B | ARG71 | electrostatic stabiliser |
B | GLU74 | electrostatic stabiliser, modifies pKa |
B | CYS100 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
B | HIS101 | electrostatic stabiliser, proton acceptor, proton donor |
B | TYR120 | electrostatic stabiliser |
site_id | MCSA3 |
Number of Residues | 6 |
Details | M-CSA 964 |
Chain | Residue | Details |
C | GLY70 | electrostatic stabiliser |
C | ARG71 | electrostatic stabiliser |
C | GLU74 | electrostatic stabiliser, modifies pKa |
C | CYS100 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
C | HIS101 | electrostatic stabiliser, proton acceptor, proton donor |
C | TYR120 | electrostatic stabiliser |