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 | 0016787 | molecular_function | hydrolase 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 | 0016787 | molecular_function | hydrolase 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 | 0016787 | molecular_function | hydrolase 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 | 0016787 | molecular_function | hydrolase 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 | 0016787 | molecular_function | hydrolase 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 | 0016787 | molecular_function | hydrolase 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 | 0016787 | molecular_function | hydrolase 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 | 0016787 | molecular_function | hydrolase 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 | 0016787 | molecular_function | hydrolase 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 | 0016787 | molecular_function | hydrolase 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 | 0016787 | molecular_function | hydrolase 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 | 0016787 | molecular_function | hydrolase 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 | 1980 |
| Details | Domain: {"description":"PfpI endopeptidase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00608","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"11114201","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00608","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
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 |
