4IEF
Complex of Porphyromonas gingivalis RgpB pro- and mature domains
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0008234 | molecular_function | cysteine-type peptidase activity |
| C | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| D | 0006508 | biological_process | proteolysis |
| D | 0008233 | molecular_function | peptidase activity |
| D | 0008234 | molecular_function | cysteine-type peptidase activity |
| E | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| F | 0006508 | biological_process | proteolysis |
| F | 0008233 | molecular_function | peptidase activity |
| F | 0008234 | molecular_function | cysteine-type peptidase activity |
| G | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| H | 0006508 | biological_process | proteolysis |
| H | 0008233 | molecular_function | peptidase activity |
| H | 0008234 | molecular_function | cysteine-type peptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 301 |
| Chain | Residue |
| A | ALA99 |
| A | GLN200 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BA B 701 |
| Chain | Residue |
| B | GLU390 |
| B | HIS395 |
| B | ASP521 |
| B | HOH916 |
| B | HOH917 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 702 |
| Chain | Residue |
| B | ASP332 |
| B | TYR334 |
| B | GLU336 |
| B | HOH831 |
| A | ILE159 |
| B | VAL329 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 703 |
| Chain | Residue |
| B | ASP307 |
| B | PHE478 |
| B | GLU487 |
| B | HOH845 |
| B | HOH846 |
| B | HOH847 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 704 |
| Chain | Residue |
| B | ASP613 |
| B | GLU639 |
| D | HOH816 |
| D | HOH917 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA B 705 |
| Chain | Residue |
| B | ASP614 |
| B | HOH813 |
| D | ASP614 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE TRS B 706 |
| Chain | Residue |
| B | GLU254 |
| B | ASP258 |
| B | ASP614 |
| B | HOH949 |
| D | GLU254 |
| D | ASP258 |
| D | ASP614 |
| D | HOH914 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BA D 701 |
| Chain | Residue |
| D | GLU390 |
| D | HIS395 |
| D | ASP521 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 702 |
| Chain | Residue |
| D | ASP307 |
| D | PHE478 |
| D | GLU487 |
| D | HOH832 |
| D | HOH833 |
| D | HOH898 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 703 |
| Chain | Residue |
| C | ILE159 |
| D | VAL329 |
| D | ASP332 |
| D | TYR334 |
| D | GLU336 |
| D | HOH834 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA D 704 |
| Chain | Residue |
| B | HOH815 |
| B | HOH947 |
| D | ASP613 |
| D | GLU639 |
| D | HOH899 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BA F 701 |
| Chain | Residue |
| F | GLU390 |
| F | HIS395 |
| F | ASP521 |
| F | HOH876 |
| F | HOH877 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA F 702 |
| Chain | Residue |
| E | ILE159 |
| F | VAL329 |
| F | ASP332 |
| F | TYR334 |
| F | GLU336 |
| F | HOH817 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA F 703 |
| Chain | Residue |
| F | ASP307 |
| F | PHE478 |
| F | GLU487 |
| F | HOH836 |
| F | HOH837 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA F 704 |
| Chain | Residue |
| F | ASP613 |
| F | GLU639 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA F 705 |
| Chain | Residue |
| F | ASP614 |
| H | ASP614 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA F 706 |
| Chain | Residue |
| F | GLU254 |
| F | HOH810 |
| H | ASP258 |
| H | HOH911 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA F 707 |
| Chain | Residue |
| F | ASP616 |
| F | HOH829 |
| F | HOH929 |
| H | ASP255 |
| H | HOH921 |
| H | HOH922 |
| site_id | CC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA F 708 |
| Chain | Residue |
| F | ASP258 |
| H | GLU254 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BA H 701 |
| Chain | Residue |
| H | GLU390 |
| H | HIS395 |
| H | ASP521 |
| H | HOH876 |
| H | HOH877 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA H 702 |
| Chain | Residue |
| G | ILE159 |
| H | VAL329 |
| H | ASP332 |
| H | TYR334 |
| H | GLU336 |
| H | HOH825 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA H 703 |
| Chain | Residue |
| H | GLU487 |
| H | GOL706 |
| H | HOH839 |
| H | ASP307 |
| H | PHE478 |
| site_id | CC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA H 704 |
| Chain | Residue |
| H | ASP613 |
| H | GLU639 |
| site_id | CC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG H 705 |
| Chain | Residue |
| F | ASP614 |
| F | HOH810 |
| F | HOH929 |
| H | GLU254 |
| H | ASP258 |
| site_id | CC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL H 706 |
| Chain | Residue |
| H | ASP307 |
| H | GLU345 |
| H | PHE478 |
| H | TYR480 |
| H | ASN481 |
| H | VAL482 |
| H | PRO483 |
| H | CA703 |
| H | HOH839 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"10523290","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1CVR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"23558682","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10523290","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1CVR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1CVR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1CVR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4IEF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"4IEF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 806 |
| Chain | Residue | Details |
| B | GLU381 | electrostatic stabiliser |
| B | HIS440 | proton acceptor, proton donor |
| B | GLY441 | electrostatic stabiliser |
| B | VAL474 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 806 |
| Chain | Residue | Details |
| D | GLU381 | electrostatic stabiliser |
| D | HIS440 | proton acceptor, proton donor |
| D | GLY441 | electrostatic stabiliser |
| D | VAL474 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 806 |
| Chain | Residue | Details |
| F | GLU381 | electrostatic stabiliser |
| F | HIS440 | proton acceptor, proton donor |
| F | GLY441 | electrostatic stabiliser |
| F | VAL474 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 806 |
| Chain | Residue | Details |
| H | GLU381 | electrostatic stabiliser |
| H | HIS440 | proton acceptor, proton donor |
| H | GLY441 | electrostatic stabiliser |
| H | VAL474 | electrostatic stabiliser |






