6F2H
Structure of Protease 1 from Pyrococcus horikoshii co-crystallized in presence of 10 mM Tb-Xo4 and potassium iodide.
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 |
D | 0005737 | cellular_component | cytoplasm |
D | 0006508 | biological_process | proteolysis |
D | 0008233 | molecular_function | peptidase activity |
D | 0036524 | molecular_function | protein deglycase activity |
E | 0005737 | cellular_component | cytoplasm |
E | 0006508 | biological_process | proteolysis |
E | 0008233 | molecular_function | peptidase activity |
E | 0036524 | molecular_function | protein deglycase activity |
F | 0005737 | cellular_component | cytoplasm |
F | 0006508 | biological_process | proteolysis |
F | 0008233 | molecular_function | peptidase activity |
F | 0036524 | molecular_function | protein deglycase activity |
G | 0005737 | cellular_component | cytoplasm |
G | 0006508 | biological_process | proteolysis |
G | 0008233 | molecular_function | peptidase activity |
G | 0036524 | molecular_function | protein deglycase activity |
H | 0005737 | cellular_component | cytoplasm |
H | 0006508 | biological_process | proteolysis |
H | 0008233 | molecular_function | peptidase activity |
H | 0036524 | molecular_function | protein deglycase activity |
I | 0005737 | cellular_component | cytoplasm |
I | 0006508 | biological_process | proteolysis |
I | 0008233 | molecular_function | peptidase activity |
I | 0036524 | molecular_function | protein deglycase activity |
J | 0005737 | cellular_component | cytoplasm |
J | 0006508 | biological_process | proteolysis |
J | 0008233 | molecular_function | peptidase activity |
J | 0036524 | molecular_function | protein deglycase activity |
K | 0005737 | cellular_component | cytoplasm |
K | 0006508 | biological_process | proteolysis |
K | 0008233 | molecular_function | peptidase activity |
K | 0036524 | molecular_function | protein deglycase activity |
L | 0005737 | cellular_component | cytoplasm |
L | 0006508 | biological_process | proteolysis |
L | 0008233 | molecular_function | peptidase activity |
L | 0036524 | molecular_function | protein deglycase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | binding site for residue 7MT A 201 |
Chain | Residue |
A | ALA8 |
A | ASN9 |
A | PHE35 |
A | GLU36 |
A | ARG75 |
A | IOD202 |
A | HOH338 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue IOD A 202 |
Chain | Residue |
A | ASN9 |
A | 7MT201 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue 7MT B 201 |
Chain | Residue |
B | ALA8 |
B | ASN9 |
B | PHE35 |
B | GLU36 |
B | ARG75 |
B | IOD202 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue IOD B 202 |
Chain | Residue |
B | ASN9 |
B | ARG75 |
B | 7MT201 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue TB C 201 |
Chain | Residue |
C | IOD202 |
C | HOH370 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue IOD C 202 |
Chain | Residue |
C | ASN9 |
C | ARG75 |
C | TB201 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue TB E 201 |
Chain | Residue |
E | GLU160 |
E | HOH317 |
site_id | AC8 |
Number of Residues | 1 |
Details | binding site for residue TB E 202 |
Chain | Residue |
E | GLU133 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue 7MT E 203 |
Chain | Residue |
E | ALA8 |
E | ASN9 |
E | PHE35 |
E | GLU36 |
E | ARG75 |
E | IOD204 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue IOD E 204 |
Chain | Residue |
E | ASN9 |
E | 7MT203 |
site_id | AD2 |
Number of Residues | 2 |
Details | binding site for residue TB F 202 |
Chain | Residue |
F | GLU29 |
F | HOH349 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue 7MT F 203 |
Chain | Residue |
F | ALA8 |
F | ASN9 |
F | PHE35 |
F | GLU36 |
F | ARG75 |
F | IOD204 |
site_id | AD4 |
Number of Residues | 2 |
Details | binding site for residue IOD F 204 |
Chain | Residue |
F | ASN9 |
F | 7MT203 |
site_id | AD5 |
Number of Residues | 6 |
Details | binding site for residue 7MT G 201 |
Chain | Residue |
G | ALA8 |
G | ASN9 |
G | PHE35 |
G | GLU36 |
G | ARG75 |
G | IOD202 |
site_id | AD6 |
Number of Residues | 2 |
Details | binding site for residue IOD G 202 |
Chain | Residue |
G | ASN9 |
G | 7MT201 |
site_id | AD7 |
Number of Residues | 1 |
Details | binding site for residue TB H 201 |
Chain | Residue |
H | IOD202 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue IOD H 202 |
Chain | Residue |
H | ASN9 |
H | ARG75 |
H | TB201 |
site_id | AD9 |
Number of Residues | 6 |
Details | binding site for residue 7MT I 201 |
Chain | Residue |
I | ALA8 |
I | ASN9 |
I | PHE35 |
I | GLU36 |
I | ARG75 |
I | IOD202 |
site_id | AE1 |
Number of Residues | 3 |
Details | binding site for residue IOD I 202 |
Chain | Residue |
I | ASN9 |
I | ARG75 |
I | 7MT201 |
site_id | AE2 |
Number of Residues | 1 |
Details | binding site for residue TB J 201 |
Chain | Residue |
J | HOH326 |
site_id | AE3 |
Number of Residues | 6 |
Details | binding site for residue 7MT J 202 |
Chain | Residue |
J | ALA8 |
J | ASN9 |
J | PHE35 |
J | GLU36 |
J | ARG75 |
J | IOD203 |
site_id | AE4 |
Number of Residues | 2 |
Details | binding site for residue IOD J 203 |
Chain | Residue |
J | ASN9 |
J | 7MT202 |
site_id | AE5 |
Number of Residues | 1 |
Details | binding site for residue TB K 201 |
Chain | Residue |
K | GLU60 |
site_id | AE6 |
Number of Residues | 6 |
Details | binding site for residue 7MT K 202 |
Chain | Residue |
K | ALA8 |
K | ASN9 |
K | PHE35 |
K | GLU36 |
K | ARG75 |
K | IOD203 |
site_id | AE7 |
Number of Residues | 1 |
Details | binding site for residue IOD K 203 |
Chain | Residue |
K | 7MT202 |
site_id | AE8 |
Number of Residues | 6 |
Details | binding site for residue 7MT L 201 |
Chain | Residue |
L | ALA8 |
L | ASN9 |
L | PHE35 |
L | GLU36 |
L | ARG75 |
L | IOD202 |
site_id | AE9 |
Number of Residues | 2 |
Details | binding site for residue IOD L 202 |
Chain | Residue |
L | ASN9 |
L | 7MT201 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:11114201 |
Chain | Residue | Details |
A | CYS100 | |
J | CYS100 | |
K | CYS100 | |
L | CYS100 | |
B | CYS100 | |
C | CYS100 | |
D | CYS100 | |
E | CYS100 | |
F | CYS100 | |
G | CYS100 | |
H | CYS100 | |
I | CYS100 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00608 |
Chain | Residue | Details |
A | HIS101 | |
J | HIS101 | |
K | HIS101 | |
L | HIS101 | |
B | HIS101 | |
C | HIS101 | |
D | HIS101 | |
E | HIS101 | |
F | HIS101 | |
G | HIS101 | |
H | HIS101 | |
I | 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 | MCSA10 |
Number of Residues | 6 |
Details | M-CSA 964 |
Chain | Residue | Details |
J | GLY70 | electrostatic stabiliser |
J | ARG71 | electrostatic stabiliser |
J | GLU74 | electrostatic stabiliser, modifies pKa |
J | CYS100 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
J | HIS101 | electrostatic stabiliser, proton acceptor, proton donor |
J | TYR120 | electrostatic stabiliser |
site_id | MCSA11 |
Number of Residues | 6 |
Details | M-CSA 964 |
Chain | Residue | Details |
K | GLY70 | electrostatic stabiliser |
K | ARG71 | electrostatic stabiliser |
K | GLU74 | electrostatic stabiliser, modifies pKa |
K | CYS100 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
K | HIS101 | electrostatic stabiliser, proton acceptor, proton donor |
K | TYR120 | electrostatic stabiliser |
site_id | MCSA12 |
Number of Residues | 6 |
Details | M-CSA 964 |
Chain | Residue | Details |
L | GLY70 | electrostatic stabiliser |
L | ARG71 | electrostatic stabiliser |
L | GLU74 | electrostatic stabiliser, modifies pKa |
L | CYS100 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
L | HIS101 | electrostatic stabiliser, proton acceptor, proton donor |
L | 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 |
site_id | MCSA4 |
Number of Residues | 6 |
Details | M-CSA 964 |
Chain | Residue | Details |
D | GLY70 | electrostatic stabiliser |
D | ARG71 | electrostatic stabiliser |
D | GLU74 | electrostatic stabiliser, modifies pKa |
D | CYS100 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
D | HIS101 | electrostatic stabiliser, proton acceptor, proton donor |
D | TYR120 | electrostatic stabiliser |
site_id | MCSA5 |
Number of Residues | 6 |
Details | M-CSA 964 |
Chain | Residue | Details |
E | GLY70 | electrostatic stabiliser |
E | ARG71 | electrostatic stabiliser |
E | GLU74 | electrostatic stabiliser, modifies pKa |
E | CYS100 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
E | HIS101 | electrostatic stabiliser, proton acceptor, proton donor |
E | TYR120 | electrostatic stabiliser |
site_id | MCSA6 |
Number of Residues | 6 |
Details | M-CSA 964 |
Chain | Residue | Details |
F | GLY70 | electrostatic stabiliser |
F | ARG71 | electrostatic stabiliser |
F | GLU74 | electrostatic stabiliser, modifies pKa |
F | CYS100 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
F | HIS101 | electrostatic stabiliser, proton acceptor, proton donor |
F | TYR120 | electrostatic stabiliser |
site_id | MCSA7 |
Number of Residues | 6 |
Details | M-CSA 964 |
Chain | Residue | Details |
G | GLY70 | electrostatic stabiliser |
G | ARG71 | electrostatic stabiliser |
G | GLU74 | electrostatic stabiliser, modifies pKa |
G | CYS100 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
G | HIS101 | electrostatic stabiliser, proton acceptor, proton donor |
G | TYR120 | electrostatic stabiliser |
site_id | MCSA8 |
Number of Residues | 6 |
Details | M-CSA 964 |
Chain | Residue | Details |
H | GLY70 | electrostatic stabiliser |
H | ARG71 | electrostatic stabiliser |
H | GLU74 | electrostatic stabiliser, modifies pKa |
H | CYS100 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
H | HIS101 | electrostatic stabiliser, proton acceptor, proton donor |
H | TYR120 | electrostatic stabiliser |
site_id | MCSA9 |
Number of Residues | 6 |
Details | M-CSA 964 |
Chain | Residue | Details |
I | GLY70 | electrostatic stabiliser |
I | ARG71 | electrostatic stabiliser |
I | GLU74 | electrostatic stabiliser, modifies pKa |
I | CYS100 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
I | HIS101 | electrostatic stabiliser, proton acceptor, proton donor |
I | TYR120 | electrostatic stabiliser |